MUTAFY

Mutafy result for your input
6d2d346d33bc454595719f83d2bbaf85

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Length

Two pieces of information are presented here to help you choose: the first is the length of the protein and the second is the partners if any in the structure.

Clicking on an entry in the PDB, AlphaFold2 or Swissmodel tracks (if structures are present) will load that protein structure.

Best Mutant and Wildtype Protein Structures for your Input Genes

Click on a row of the table to load a given protein structure and show additional structural and variant information.

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The table below has 6 tabs (Summary, SAV, Unique Sequences, Any Mutation, Wildtype and AlphaFold WT Predictions).

In each tab the corresponding highest quality experimentally solved protein structures are listed for all the input genes.

The search bar allows users to filter data in the table, e.g. only show data for one specific gene of interest.

Explanation of the 4 main tabs:
SAV
Lists the best structure per single amino acid variant (SAV).
Mutafy identifies all protein structures associated with the input genes with a single amino acid variant (SAV), i.e. structures which have only one amino acid substitution in their sequence compared to the canonical protein sequence (WT), and will list the best available structures for each SAV available in the PDB.

Unique Sequences
Lists the best structure per unique sequence / combination of mutations.
Mutafy identifies all protein structures associated with the input genes and will list the best available structure for each unique sequence in the PDB, including WT and SAV structures if available.

Any Mutation
Lists the best structure per any identified mutation (irrespective of other mutations).
Mutafy identifies all protein structures associated with the input genes and will list the best available structure for each mutated residue found in any of the PDB structures (regardless of other mutations in the structure), including SAV structures if available.

Wildtype
Lists all available wildtype structures.
Mutafy identifies all available WT structures associated with the input genes and will list all available WT structures with the best structures at the top of the table.

Input Information
Genes of interest	SOD1; PRPS1
Minimum relative sequence length	0.50
Minimum HSP coverage	0.1
Minimum relative wide type length	0.90
Number of top structures	1

Gene 1	SOD1
Total number of structures	139
Total number of SAV	19
Total number of unique sequences	53
Total number of variants	177
Total number of clinvar variants	14
Total number of WTs	42

Gene 2	PRPS1
Total number of structures	25
Total number of SAV	9
Total number of unique sequences	10
Total number of variants	9
Total number of clinvar variants	5
Total number of WTs	15

Gene	AA position	Mutation	PDB ID	Chain	Resolution	Structure method	% unsolved residues	Clinical Significance	Associated traits	Download	External databases
PRPS1	43	E43T	4lyg	A, B	3.00 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 4.9 %	NA	NA	cif fasta pdb	NA
PRPS1	52	D52H	4f8e	A, B	2.27 Å	X-RAY DIFFRACTION	A: 5.5 %, B: 5.5 %	Pathogenic	Phosphoribosylpyrophosphate synthetase superactivity	cif fasta pdb	['Orphanet: 3222', 'MedGen: C1970827', 'MONDO: MONDO:0010395', 'OMIM: 300661']
PRPS1	65	D65N	4lzn	A, B	2.14 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Pathogenic	Hearing loss, X-linked 1	cif fasta pdb	['Orphanet: 90625', 'MedGen: C1844677', 'MONDO: MONDO:0010577', 'OMIM: 304500']
PRPS1	87	A87T	4lzo	A, B	3.31 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Uncertain significance	Charcot-Marie-Tooth Neuropathy X	cif fasta pdb	['MedGen: CN118851']
PRPS1	115	M115T	4m0p	A, B	2.11 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Likely pathogenic	Charcot-Marie-Tooth Neuropathy X	cif fasta pdb	['MedGen: CN118851']
PRPS1	132	S132A	2h07	A, B	2.20 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	NA	NA	cif fasta pdb	NA
PRPS1	133	Q133P	4m0u	A, B	2.74 Å	X-RAY DIFFRACTION	A: 7.1 %, B: 5.5 %	Pathogenic	Arts syndrome	cif fasta pdb	['Orphanet: 1187', 'MedGen: C0796028', 'MONDO: MONDO:0010533', 'OMIM: 301835']
PRPS1	146	Y146M	2h08	A, B	2.50 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	NA	NA	cif fasta pdb	NA
PRPS1	306	E306A	8dbn	A, B, C, D, E, F	2.40 Å	ELECTRON MICROSCOPY	A: 4.4 %, B: 4.4 %, C: 4.4 %, D: 4.4 %, E: 4.4 %, F: 4.4 %	NA	NA	cif fasta pdb	NA
SOD1	2	T2D	5k02	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	1.99 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA, M: NA, N: NA, O: NA, P: NA, Q: NA, R: NA, S: NA, T: NA, U: NA, V: NA, W: NA, X: NA	NA	NA	cif fasta pdb	NA
SOD1	4	A4V	6z3v	A, B	1.25 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	5	A5V	6spi	A, B, C, D, E, F, G, H, I, J, K, L	2.80 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %, K: 0.6 %, L: 0.6 %	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	6	C6A	5j0f	A, B	1.25 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	37	G37R	1azv	A, B	1.90 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Motor neuron disease	cif fasta pdb	['Orphanet: 98503', 'MedGen: C0085084', 'MONDO: MONDO:0020128']
SOD1	38	L38V	2wyt	A, B	1.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	Likely pathogenic	not provided, Amyotrophic lateral sclerosis type 1	cif fasta pdb	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	46	H46R	1oez	A, B, C, D	2.15 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided, Amyotrophic lateral sclerosis	cif fasta pdb	['Orphanet: 803', 'MedGen: C0002736', 'MONDO: MONDO:0004976', 'OMIM: 105400', 'Human Phenotype Ontology: HP:0007354']
SOD1	54	T54R	3ecw	A, B, C, D	2.15 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 19.0 %, D: 19.6 %	NA	NA	cif fasta pdb	NA
SOD1	57	C57S	4mcm	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 0.7 %, D: NA, E: 0.7 %, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	77	E77A	8gsq	E, G	2.10 Å	X-RAY DIFFRACTION	E: NA, G: 13.6 %	NA	NA	cif fasta pdb	NA
SOD1	80	H80R	3qqd	A	1.65 Å	X-RAY DIFFRACTION	A: 20.1 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	85	G85R	2vr6	A, B	1.30 Å	X-RAY DIFFRACTION	A: NA, B: NA	Likely pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	86	G86R	2zkw	A, B	1.90 Å	X-RAY DIFFRACTION	A: 6.3 %, B: 8.2 %	Likely pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	93	G93A	7t8g	A, B	1.35 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	94	G94A	2zky	A, B, C, D, E, F, G, H, I, J	2.40 Å	X-RAY DIFFRACTION	A: 4.4 %, B: 4.4 %, C: 3.8 %, D: 3.8 %, E: 3.8 %, F: 3.8 %, G: 3.8 %, H: 3.8 %, I: 3.8 %, J: 3.8 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	113	I113T	4a7u	A, B	0.98 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	124	D124V	3h2p	A, B	1.55 Å	X-RAY DIFFRACTION	A: 17.6 %, B: 15.7 %	NA	NA	cif fasta pdb	NA
SOD1	125	D125H	1p1v	A, B, C	1.40 Å	X-RAY DIFFRACTION	A: 4.6 %, B: 5.9 %, C: 4.6 %	NA	NA	cif fasta pdb	NA
SOD1	134	S134N	1ozu	A, B	1.30 Å	X-RAY DIFFRACTION	A: 2.0 %, B: 17.0 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Gene	AA substitutions	Close AA substitutions	PDB ID	Chain	Resolution	Structure method	% unsolved residues	Clinical Significance	Associated traits	Download	External databases
PRPS1			8dbi	A, B, C, D, E, F	2.00 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %	NA	NA	cif fasta pdb	NA
PRPS1		S132A	2h07	A, B	2.20 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	NA	NA	cif fasta pdb	NA
PRPS1	Y146M		2h08	A, B	2.50 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	NA	NA	cif fasta pdb	NA
PRPS1	D52H		4f8e	A, B	2.27 Å	X-RAY DIFFRACTION	A: 5.5 %, B: 5.5 %	Pathogenic	Phosphoribosylpyrophosphate synthetase superactivity	cif fasta pdb	['Orphanet: 3222', 'MedGen: C1970827', 'MONDO: MONDO:0010395', 'OMIM: 300661']
PRPS1	E43T		4lyg	A, B	3.00 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 4.9 %	NA	NA	cif fasta pdb	NA
PRPS1		D65N	4lzn	A, B	2.14 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Pathogenic	Hearing loss, X-linked 1	cif fasta pdb	['Orphanet: 90625', 'MedGen: C1844677', 'MONDO: MONDO:0010577', 'OMIM: 304500']
PRPS1	A87T		4lzo	A, B	3.31 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Uncertain significance	Charcot-Marie-Tooth Neuropathy X	cif fasta pdb	['MedGen: CN118851']
PRPS1	M115T		4m0p	A, B	2.11 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Likely pathogenic	Charcot-Marie-Tooth Neuropathy X	cif fasta pdb	['MedGen: CN118851']
PRPS1	Q133P		4m0u	A, B	2.74 Å	X-RAY DIFFRACTION	A: 7.1 %, B: 5.5 %	Pathogenic	Arts syndrome	cif fasta pdb	['Orphanet: 1187', 'MedGen: C0796028', 'MONDO: MONDO:0010533', 'OMIM: 301835']
PRPS1	E306A		8dbn	A, B, C, D, E, F	2.40 Å	ELECTRON MICROSCOPY	A: 4.4 %, B: 4.4 %, C: 4.4 %, D: 4.4 %, E: 4.4 %, F: 4.4 %	NA	NA	cif fasta pdb	NA
SOD1	G37R		1azv	A, B	1.90 Å	X-RAY DIFFRACTION	A: nan, B: nan	Pathogenic	Motor neuron disease	cif fasta pdb	['Orphanet: 98503', 'MedGen: C0085084', 'MONDO: MONDO:0020128']
SOD1	C6A, F50E, G51E, C111S	E133Q	1mfm	A	1.02 Å	X-RAY DIFFRACTION	A: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, F50E, G51E, C111S, V148K, I151K		1dsw	A	999.00 Å	SOLUTION NMR	A: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, C111S	K136E	1fun	A, B, C, D, E, F, G, H, I, J	2.85 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan	NA	NA	cif fasta pdb	NA
SOD1			2c9v	A, B	1.07 Å	X-RAY DIFFRACTION	A: nan, B: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, C111S		1sos	A, B, C, D, E, F, G, H, I, J	2.50 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan	NA	NA	cif fasta pdb	NA
SOD1	C7A, C112S		1n18	A, B, C, D, E, F, G, H, I, J	2.00 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %	NA	NA	cif fasta pdb	NA
SOD1	A5V, C7A, C112S		1n19	A, B	1.86 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	H46R		1oez	A, B, C, D	2.15 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided, Amyotrophic lateral sclerosis	cif fasta pdb	['Orphanet: 803', 'MedGen: C0002736', 'MONDO: MONDO:0004976', 'OMIM: 105400', 'Human Phenotype Ontology: HP:0007354']
SOD1		S134N	1ozu	A, B	1.30 Å	X-RAY DIFFRACTION	A: 2.0 %, B: 17.0 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	D125H		1p1v	A, B, C	1.40 Å	X-RAY DIFFRACTION	A: 4.6 %, B: 5.9 %, C: 4.6 %	NA	NA	cif fasta pdb	NA
SOD1	C6A, H43R, C111S		1ptz	A, B	1.80 Å	X-RAY DIFFRACTION	A: nan, B: nan	Pathogenic	not provided, Amyotrophic lateral sclerosis type 1	cif fasta pdb	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	I113T		4a7u	A, B	0.98 Å	X-RAY DIFFRACTION	A: nan, B: nan	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	A4V		6z3v	A, B	1.25 Å	X-RAY DIFFRACTION	A: nan, B: nan	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	C6A, C111A		2gbt	A, B, C, D	1.70 Å	X-RAY DIFFRACTION	A: 0.7 %, B: 0.7 %, C: 17.6 %, D: 19.0 %	NA	NA	cif fasta pdb	NA
SOD1	C6A, C57A, C111A, C146A		2gbu	A, B, C, D	2.00 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: 19.0 %, D: 19.6 %	NA	NA	cif fasta pdb	NA
SOD1	H46R, H48Q		3k91	A, B	1.75 Å	X-RAY DIFFRACTION	A: 3.3 %, B: 16.3 %	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided, Amyotrophic lateral sclerosis	cif fasta pdb	['Orphanet: 803', 'MedGen: C0002736', 'MONDO: MONDO:0004976', 'OMIM: 105400', 'Human Phenotype Ontology: HP:0007354']
SOD1	C7A, H81S, D84S, C112S		2r27	A, B	2.00 Å	X-RAY DIFFRACTION	A: 13.0 %, B: 13.0 %	NA	NA	cif fasta pdb	NA
SOD1	G85R		2vr6	A, B	1.30 Å	X-RAY DIFFRACTION	A: nan, B: nan	Likely pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	G93A		7t8g	A, B	1.35 Å	X-RAY DIFFRACTION	A: nan, B: nan	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1		L38V	2wyt	A, B	1.00 Å	X-RAY DIFFRACTION	A: nan, B: nan	Likely pathogenic	not provided, Amyotrophic lateral sclerosis type 1	cif fasta pdb	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	C6A, F50E, G51E, C111A		2xjk	A	1.45 Å	X-RAY DIFFRACTION	A: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, H46S, H48S, F50E, G51E, C111A, H120S		2xjl	A	1.55 Å	X-RAY DIFFRACTION	A: nan	NA	NA	cif fasta pdb	NA
SOD1	G86R		2zkw	A, B	1.90 Å	X-RAY DIFFRACTION	A: 6.3 %, B: 8.2 %	Likely pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	G94A		2zky	A, B, C, D, E, F, G, H, I, J	2.40 Å	X-RAY DIFFRACTION	A: 4.4 %, B: 4.4 %, C: 3.8 %, D: 3.8 %, E: 3.8 %, F: 3.8 %, G: 3.8 %, H: 3.8 %, I: 3.8 %, J: 3.8 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	T54R		3ecw	A, B, C, D	2.15 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: 19.0 %, D: 19.6 %	NA	NA	cif fasta pdb	NA
SOD1	D90G, S102R, C111S, A123Q	D96N, D109E, L117M	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan	Uncertain significance	not provided	cif fasta pdb	['MedGen: CN517202']
SOD1	D124V		3h2p	A, B	1.55 Å	X-RAY DIFFRACTION	A: 17.6 %, B: 15.7 %	NA	NA	cif fasta pdb	NA
SOD1	H80R		3qqd	A	1.65 Å	X-RAY DIFFRACTION	A: 20.1 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	C6A, F50E, G51E, H63S, H71S, H80S, D83S, C111A		3hff	A	2.20 Å	X-RAY DIFFRACTION	A: 24.8 %	NA	NA	cif fasta pdb	NA
SOD1	T2M, I17T, E24A, N26G, G27E, K30V, W32S, S34Q, K36T, L42Q, A55Q, L67H, K75A	N19H, V31L, E49Q, F50Y, R69K	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: 2.0 %, D: 0.7 %, E: nan, F: nan	NA	NA	cif fasta pdb	NA
SOD1	I99T, I113T		4a7g	A	1.24 Å	X-RAY DIFFRACTION	A: nan	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	C6A, H43F, F50E, G51E, C111A		4bcy	A	1.27 Å	X-RAY DIFFRACTION	A: 4.6 %	NA	NA	cif fasta pdb	NA
SOD1	C6A, E49G, F50A, C111S, K128A, C146S		4bcz	A, B	1.93 Å	X-RAY DIFFRACTION	A: nan, B: 0.9 %	NA	NA	cif fasta pdb	NA
SOD1	C6A, H43F, E49G, F50A, C111S, K128A, C146S		4bd4	A, B, C, D, E, F, G, H, I	2.78 Å	X-RAY DIFFRACTION	A: 0.9 %, B: 0.9 %, C: 1.8 %, D: 5.5 %, E: 5.5 %, F: 7.3 %, G: 2.7 %, H: 9.1 %, I: 10.9 %	NA	NA	cif fasta pdb	NA
SOD1	C57S		4mcm	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: 0.7 %, D: nan, E: 0.7 %, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, C111S, I149T		4oh2	A, B, C, D, E, F, G, H, I, J	2.38 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, I35A, E49G, F50A, C111S, K128A, C146S		4xcr	A, B	3.60 Å	X-RAY DIFFRACTION	A: nan, B: nan	NA	NA	cif fasta pdb	NA
SOD1	E37G, F38A, C99S, K116A, C134S		5j07	A, B	2.00 Å	X-RAY DIFFRACTION	A: nan, B: nan	NA	NA	cif fasta pdb	NA
SOD1	E22G, F23A, C84S, K101A, C119S		5j0c	A, B	1.60 Å	X-RAY DIFFRACTION	A: 1.8 %, B: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A		5j0f	A, B	1.25 Å	X-RAY DIFFRACTION	A: nan, B: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, E49G, F50A, C111S		5j0g	A, B	2.50 Å	X-RAY DIFFRACTION	A: nan, B: nan	NA	NA	cif fasta pdb	NA
SOD1	T2D		5k02	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	1.99 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan, M: nan, N: nan, O: nan, P: nan, Q: nan, R: nan, S: nan, T: nan, U: nan, V: nan, W: nan, X: nan	NA	NA	cif fasta pdb	NA
SOD1	K3N, T6P, L10N, G12H, F13A, H14S, F18K, N21V, A23K, C25V, T26E, A28T	S1T, I2V, L5V, H11Y, V15I, T22S	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	D84S, C112S		6dtk	A, B, C, D, E	2.00 Å	X-RAY DIFFRACTION	A: 3.4 %, B: nan, C: nan, D: nan, E: nan	NA	NA	cif fasta pdb	NA
SOD1	C6A, F50E, C111S, K128A, C146S		6flh	A	1.79 Å	X-RAY DIFFRACTION	A: nan	NA	NA	cif fasta pdb	NA
SOD1	C57A, C146A		6foi	A, B, C, D, E, F, G, H, I, J, K, L	2.00 Å	X-RAY DIFFRACTION	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan	NA	NA	cif fasta pdb	NA
SOD1	C3A, K6G, D8P, P10T, N16R, E18L, K20L, E21T, S22P, N23E, P25R, V26C, K27L, W29E, K33D, T36E, E37P, F42L, N50L, A52N, G53N, T55N, A57C, P59N, L64D, S65G, R66A, K67S, E74S, V78R, T85R, K88A, V91R, D93I, V94F, S95R, S99E, V100Q, S102K, S104W, G105D, H117D, K119G, A120E, E129P, E130L, T132K, K133I, S139E	V4I, I14V, I15V, V28I, S31T, E46Q, F47Y, K72Q, E75D, I96M, I101L, L103V, I109V, T113S, V115I, V116I, K125R, N128H, A137S, V145I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: nan, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	C3A, K6G, D8P, P10T, N16R, E18L, K20L, E21T, S22P, N23E, G24R, P25C, W29E, K33D, T36E, E37P, F42L, N50L, A52N, G53N, T55N, A57C, P59N, L64D, S65G, R66A, K67S, E74S, V78R, T85R, K88A, V91R, D93I, V94F, S95R, S99E, V100Q, S102K, S104W, G105D, H117D, K119G, A120E, E129P, E130L, T132K, K133I, S139E	V4I, I14V, I15V, V26L, V28I, S31T, E46Q, F47Y, K72Q, E75D, I96M, I101L, L103V, I109V, T113S, V115I, V116I, K125R, N128H, A137S, V145I	6fp6	B, D, F, H, J, L, N, P, R, T, V, X	3.00 Å	X-RAY DIFFRACTION	B: 15.7 %, D: 14.6 %, F: 14.6 %, H: 16.1 %, J: 15.3 %, L: 14.6 %, N: 14.6 %, P: 15.7 %, R: 15.3 %, T: 18.6 %, V: 46.7 %, X: 15.3 %	NA	NA	cif fasta pdb	NA
SOD1	A5V		6spi	A, B, C, D, E, F, G, H, I, J, K, L	2.80 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %, K: 0.6 %, L: 0.6 %	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	C6A, H46W, E49G, F50A, C111S, K128A, C146S		7cjv	A	999.00 Å	SOLUTION NMR	A: nan	NA	NA	cif fasta pdb	NA
SOD1	C58D, C147D		7fb6	A, B	1.80 Å	X-RAY DIFFRACTION	A: 3.7 %, B: 10.6 %	NA	NA	cif fasta pdb	NA
SOD1	E77A		8gsq	E, G	2.10 Å	X-RAY DIFFRACTION	E: nan, G: 13.6 %	NA	NA	cif fasta pdb	NA

Gene	AA position	Mutation	PDB ID	Chain	Resolution	Structure method	% unsolved residues	Clinical Significance	Associated traits	Download	External databases
PRPS1	43	E43T	4lyg	A, B	3.00 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 4.9 %	NA	NA	cif fasta pdb	NA
PRPS1	52	D52H	4f8e	A, B	2.27 Å	X-RAY DIFFRACTION	A: 5.5 %, B: 5.5 %	Pathogenic	Phosphoribosylpyrophosphate synthetase superactivity	cif fasta pdb	['Orphanet: 3222', 'MedGen: C1970827', 'MONDO: MONDO:0010395', 'OMIM: 300661']
PRPS1	65	D65N	4lzn	A, B	2.14 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Pathogenic	Hearing loss, X-linked 1	cif fasta pdb	['Orphanet: 90625', 'MedGen: C1844677', 'MONDO: MONDO:0010577', 'OMIM: 304500']
PRPS1	87	A87T	4lzo	A, B	3.31 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Uncertain significance	Charcot-Marie-Tooth Neuropathy X	cif fasta pdb	['MedGen: CN118851']
PRPS1	115	M115T	4m0p	A, B	2.11 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	Likely pathogenic	Charcot-Marie-Tooth Neuropathy X	cif fasta pdb	['MedGen: CN118851']
PRPS1	132	S132A	2h07	A, B	2.20 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	NA	NA	cif fasta pdb	NA
PRPS1	133	Q133P	4m0u	A, B	2.74 Å	X-RAY DIFFRACTION	A: 7.1 %, B: 5.5 %	Pathogenic	Arts syndrome	cif fasta pdb	['Orphanet: 1187', 'MedGen: C0796028', 'MONDO: MONDO:0010533', 'OMIM: 301835']
PRPS1	146	Y146M	2h08	A, B	2.50 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	NA	NA	cif fasta pdb	NA
PRPS1	306	E306A	8dbn	A, B, C, D, E, F	2.40 Å	ELECTRON MICROSCOPY	A: 4.4 %, B: 4.4 %, C: 4.4 %, D: 4.4 %, E: 4.4 %, F: 4.4 %	NA	NA	cif fasta pdb	NA
SOD1	1	S1T	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	2	I2V	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	2	T2D	5k02	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	1.99 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA, M: NA, N: NA, O: NA, P: NA, Q: NA, R: NA, S: NA, T: NA, U: NA, V: NA, W: NA, X: NA	NA	NA	cif fasta pdb	NA
SOD1	2	T2M	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	3	C3A	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	3	K3N	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	4	A4V	6z3v	A, B	1.25 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	4	V4I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	5	A5V	1n19	A, B	1.86 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided	cif fasta pdb	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	5	L5V	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	6	C6A	1mfm	A	1.02 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	6	K6G	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	6	T6P	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	7	C7A	1n19	A, B	1.86 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %	NA	NA	cif fasta pdb	NA
SOD1	8	D8P	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	10	L10N	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	10	P10T	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	11	H11Y	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	12	G12H	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	13	F13A	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	14	H14S	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	14	I14V	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	15	I15V	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	15	V15I	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	16	N16R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	17	I17T	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	18	E18L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	18	F18K	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	19	N19H	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	20	K20L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	21	E21T	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	21	N21V	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	22	E22G	5j0c	A, B	1.60 Å	X-RAY DIFFRACTION	A: 1.8 %, B: NA	NA	NA	cif fasta pdb	NA
SOD1	22	S22P	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	22	T22S	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	23	A23K	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	23	F23A	5j0c	A, B	1.60 Å	X-RAY DIFFRACTION	A: 1.8 %, B: NA	NA	NA	cif fasta pdb	NA
SOD1	23	N23E	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	24	E24A	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	24	G24R	6fp6	B, D, F, H, J, L, N, P, R, T, V, X	3.00 Å	X-RAY DIFFRACTION	B: 15.7 %, D: 14.6 %, F: 14.6 %, H: 16.1 %, J: 15.3 %, L: 14.6 %, N: 14.6 %, P: 15.7 %, R: 15.3 %, T: 18.6 %, V: 46.7 %, X: 15.3 %	NA	NA	cif fasta pdb	NA
SOD1	25	C25V	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	25	P25C	6fp6	B, D, F, H, J, L, N, P, R, T, V, X	3.00 Å	X-RAY DIFFRACTION	B: 15.7 %, D: 14.6 %, F: 14.6 %, H: 16.1 %, J: 15.3 %, L: 14.6 %, N: 14.6 %, P: 15.7 %, R: 15.3 %, T: 18.6 %, V: 46.7 %, X: 15.3 %	NA	NA	cif fasta pdb	NA
SOD1	25	P25R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	26	N26G	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	26	T26E	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	26	V26C	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	26	V26L	6fp6	B, D, F, H, J, L, N, P, R, T, V, X	3.00 Å	X-RAY DIFFRACTION	B: 15.7 %, D: 14.6 %, F: 14.6 %, H: 16.1 %, J: 15.3 %, L: 14.6 %, N: 14.6 %, P: 15.7 %, R: 15.3 %, T: 18.6 %, V: 46.7 %, X: 15.3 %	NA	NA	cif fasta pdb	NA
SOD1	27	G27E	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	27	K27L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	28	A28T	5u9m	B, D	2.35 Å	X-RAY DIFFRACTION	B: 8.9 %, D: 5.6 %	NA	NA	cif fasta pdb	NA
SOD1	28	V28I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	29	W29E	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	30	K30V	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	31	S31T	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	31	V31L	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	32	W32S	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	33	K33D	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	34	S34Q	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	35	I35A	4xcr	A, B	3.60 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	36	K36T	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	36	T36E	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	37	E37G	5j07	A, B	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	37	E37P	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	37	G37R	1azv	A, B	1.90 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Motor neuron disease	cif fasta pdb	['Orphanet: 98503', 'MedGen: C0085084', 'MONDO: MONDO:0020128']
SOD1	38	F38A	5j07	A, B	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	38	L38V	2wyt	A, B	1.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	Likely pathogenic	not provided, Amyotrophic lateral sclerosis type 1	cif fasta pdb	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	42	F42L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	42	L42Q	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	43	H43F	4bcy	A	1.27 Å	X-RAY DIFFRACTION	A: 4.6 %	NA	NA	cif fasta pdb	NA
SOD1	43	H43R	1ptz	A, B	1.80 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	not provided, Amyotrophic lateral sclerosis type 1	cif fasta pdb	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	46	E46Q	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	46	H46R	3k91	A, B	1.75 Å	X-RAY DIFFRACTION	A: 3.3 %, B: 16.3 %	Pathogenic	Amyotrophic lateral sclerosis type 1, not provided, Amyotrophic lateral sclerosis	cif fasta pdb	['Orphanet: 803', 'MedGen: C0002736', 'MONDO: MONDO:0004976', 'OMIM: 105400', 'Human Phenotype Ontology: HP:0007354']
SOD1	46	H46S	2xjl	A	1.55 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	46	H46W	7cjv	A	999.00 Å	SOLUTION NMR	A: NA	NA	NA	cif fasta pdb	NA
SOD1	47	F47Y	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	48	H48Q	3k91	A, B	1.75 Å	X-RAY DIFFRACTION	A: 3.3 %, B: 16.3 %	NA	NA	cif fasta pdb	NA
SOD1	48	H48S	2xjl	A	1.55 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	49	E49G	4bcz	A, B	1.93 Å	X-RAY DIFFRACTION	A: NA, B: 0.9 %	NA	NA	cif fasta pdb	NA
SOD1	49	E49Q	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	50	F50A	4bcz	A, B	1.93 Å	X-RAY DIFFRACTION	A: NA, B: 0.9 %	NA	NA	cif fasta pdb	NA
SOD1	50	F50E	1mfm	A	1.02 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	50	F50Y	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	50	N50L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	51	G51E	1mfm	A	1.02 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	52	A52N	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	53	G53N	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	54	T54R	3ecw	A, B, C, D	2.15 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 19.0 %, D: 19.6 %	NA	NA	cif fasta pdb	NA
SOD1	55	A55Q	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	55	T55N	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	57	A57C	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	57	C57A	2gbu	A, B, C, D	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 19.0 %, D: 19.6 %	NA	NA	cif fasta pdb	NA
SOD1	57	C57S	4mcm	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 0.7 %, D: NA, E: 0.7 %, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	58	C58D	7fb6	A, B	1.80 Å	X-RAY DIFFRACTION	A: 3.7 %, B: 10.6 %	NA	NA	cif fasta pdb	NA
SOD1	59	P59N	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	63	H63S	3hff	A	2.20 Å	X-RAY DIFFRACTION	A: 24.8 %	NA	NA	cif fasta pdb	NA
SOD1	64	L64D	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	65	S65G	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	66	R66A	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	67	K67S	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	67	L67H	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	69	R69K	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	71	H71S	3hff	A	2.20 Å	X-RAY DIFFRACTION	A: 24.8 %	NA	NA	cif fasta pdb	NA
SOD1	72	K72Q	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	74	E74S	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	75	E75D	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	75	K75A	3ltv	A, B, C, D, E, F	2.45 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 2.0 %, D: 0.7 %, E: NA, F: NA	NA	NA	cif fasta pdb	NA
SOD1	77	E77A	8gsq	E, G	2.10 Å	X-RAY DIFFRACTION	E: NA, G: 13.6 %	NA	NA	cif fasta pdb	NA
SOD1	78	V78R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	80	H80R	3qqd	A	1.65 Å	X-RAY DIFFRACTION	A: 20.1 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	80	H80S	3hff	A	2.20 Å	X-RAY DIFFRACTION	A: 24.8 %	NA	NA	cif fasta pdb	NA
SOD1	81	H81S	2r27	A, B	2.00 Å	X-RAY DIFFRACTION	A: 13.0 %, B: 13.0 %	NA	NA	cif fasta pdb	NA
SOD1	83	D83S	3hff	A	2.20 Å	X-RAY DIFFRACTION	A: 24.8 %	NA	NA	cif fasta pdb	NA
SOD1	84	C84S	5j0c	A, B	1.60 Å	X-RAY DIFFRACTION	A: 1.8 %, B: NA	NA	NA	cif fasta pdb	NA
SOD1	84	D84S	2r27	A, B	2.00 Å	X-RAY DIFFRACTION	A: 13.0 %, B: 13.0 %	NA	NA	cif fasta pdb	NA
SOD1	85	G85R	2vr6	A, B	1.30 Å	X-RAY DIFFRACTION	A: NA, B: NA	Likely pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	85	T85R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	86	G86R	2zkw	A, B	1.90 Å	X-RAY DIFFRACTION	A: 6.3 %, B: 8.2 %	Likely pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	88	K88A	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	90	D90G	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	91	V91R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	93	D93I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	93	G93A	7t8g	A, B	1.35 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	94	G94A	2zky	A, B, C, D, E, F, G, H, I, J	2.40 Å	X-RAY DIFFRACTION	A: 4.4 %, B: 4.4 %, C: 3.8 %, D: 3.8 %, E: 3.8 %, F: 3.8 %, G: 3.8 %, H: 3.8 %, I: 3.8 %, J: 3.8 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	94	V94F	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	95	S95R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	96	D96N	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	Uncertain significance	not provided	cif fasta pdb	['MedGen: CN517202']
SOD1	96	I96M	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	99	C99S	5j07	A, B	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	99	I99T	4a7g	A	1.24 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	99	S99E	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	100	V100Q	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	101	I101L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	101	K101A	5j0c	A, B	1.60 Å	X-RAY DIFFRACTION	A: 1.8 %, B: NA	NA	NA	cif fasta pdb	NA
SOD1	102	S102K	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	102	S102R	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	103	L103V	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	104	S104W	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	105	G105D	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	109	D109E	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	109	I109V	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	111	C111A	4bcy	A	1.27 Å	X-RAY DIFFRACTION	A: 4.6 %	NA	NA	cif fasta pdb	NA
SOD1	111	C111S	1mfm	A	1.02 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	112	C112S	1n19	A, B	1.86 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %	NA	NA	cif fasta pdb	NA
SOD1	113	I113T	4a7u	A, B	0.98 Å	X-RAY DIFFRACTION	A: NA, B: NA	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	113	T113S	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	115	V115I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	116	K116A	5j07	A, B	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	116	V116I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	117	H117D	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	117	L117M	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	119	C119S	5j0c	A, B	1.60 Å	X-RAY DIFFRACTION	A: 1.8 %, B: NA	NA	NA	cif fasta pdb	NA
SOD1	119	K119G	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	120	A120E	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	120	H120S	2xjl	A	1.55 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	123	A123Q	3gtv	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	NA	NA	cif fasta pdb	NA
SOD1	124	D124V	3h2p	A, B	1.55 Å	X-RAY DIFFRACTION	A: 17.6 %, B: 15.7 %	NA	NA	cif fasta pdb	NA
SOD1	125	D125H	1p1v	A, B, C	1.40 Å	X-RAY DIFFRACTION	A: 4.6 %, B: 5.9 %, C: 4.6 %	NA	NA	cif fasta pdb	NA
SOD1	125	K125R	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	128	K128A	6flh	A	1.79 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	128	N128H	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	129	E129P	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	130	E130L	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	132	T132K	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	133	E133Q	1mfm	A	1.02 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	133	K133I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	134	C134S	5j07	A, B	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA	NA	NA	cif fasta pdb	NA
SOD1	134	S134N	1ozu	A, B	1.30 Å	X-RAY DIFFRACTION	A: 2.0 %, B: 17.0 %	Pathogenic	Amyotrophic lateral sclerosis type 1	cif fasta pdb	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']
SOD1	136	K136E	1fun	A, B, C, D, E, F, G, H, I, J	2.85 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA	NA	NA	cif fasta pdb	NA
SOD1	137	A137S	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	139	S139E	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	145	V145I	6fol	A, D, E, H	2.55 Å	X-RAY DIFFRACTION	A: 1.3 %, D: 1.3 %, E: NA, H: 1.3 %	NA	NA	cif fasta pdb	NA
SOD1	146	C146A	2gbu	A, B, C, D	2.00 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 19.0 %, D: 19.6 %	NA	NA	cif fasta pdb	NA
SOD1	146	C146S	6flh	A	1.79 Å	X-RAY DIFFRACTION	A: NA	NA	NA	cif fasta pdb	NA
SOD1	147	C147D	7fb6	A, B	1.80 Å	X-RAY DIFFRACTION	A: 3.7 %, B: 10.6 %	NA	NA	cif fasta pdb	NA
SOD1	148	V148K	1dsw	A	999.00 Å	SOLUTION NMR	A: NA	NA	NA	cif fasta pdb	NA
SOD1	149	I149T	4oh2	A, B, C, D, E, F, G, H, I, J	2.38 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA	NA	NA	cif fasta pdb	NA
SOD1	151	I151K	1dsw	A	999.00 Å	SOLUTION NMR	A: NA	NA	NA	cif fasta pdb	NA

Gene	PDB ID	Chain	Resolution	Structure method	% unsolved residues	Download
PRPS1	3s5j	A, B	2.02 Å	X-RAY DIFFRACTION	A: 6.7 %, B: 5.5 %	cif fasta pdb
PRPS1	8dbe	A, B, C, D, E, F	2.10 Å	ELECTRON MICROSCOPY	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %	cif fasta pdb
PRPS1	2h06	A, B	2.20 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	cif fasta pdb
PRPS1	2hcr	A, B	2.20 Å	X-RAY DIFFRACTION	A: 6.4 %, B: 5.5 %	cif fasta pdb
PRPS1	3efh	A, B	2.60 Å	X-RAY DIFFRACTION	A: 5.8 %, B: 5.8 %	cif fasta pdb
PRPS1	8dbc	A, B, C, D, E, F	3.20 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %	cif fasta pdb
PRPS1	8dbd	A, B, C, D, E, F, G, H, I, J, K, L	3.20 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %, G: 2.8 %, H: 2.8 %, I: 2.8 %, J: 2.8 %, K: 2.8 %, L: 2.8 %	cif fasta pdb
PRPS1	8dbi	A, B, C, D, E, F	2.00 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %	cif fasta pdb
PRPS1	8dbj	A, B, C, D, E, F, G, H, I, J, K, L	2.00 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %, G: 2.8 %, H: 2.8 %, I: 2.8 %, J: 2.8 %, K: 2.8 %, L: 2.8 %	cif fasta pdb
PRPS1	8dbk	A, B, C, D, E, F	2.10 Å	ELECTRON MICROSCOPY	A: 0.6 %, B: 0.6 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %	cif fasta pdb
PRPS1	8dbf	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	ELECTRON MICROSCOPY	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %, K: 0.6 %, L: 0.6 %	cif fasta pdb
PRPS1	8dbg	A, B, C, D, E, F	2.20 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %	cif fasta pdb
PRPS1	8dbh	A, B, C, D, E, F, G, H, I, J, K, L	2.20 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %, G: 2.8 %, H: 2.8 %, I: 2.8 %, J: 2.8 %, K: 2.8 %, L: 2.8 %	cif fasta pdb
PRPS1	8dbl	A, B, C, D, E, F	2.40 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %	cif fasta pdb
PRPS1	8dbm	A, B, C, D, E, F, G, H, I, J, K, L	2.40 Å	ELECTRON MICROSCOPY	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %, G: 2.8 %, H: 2.8 %, I: 2.8 %, J: 2.8 %, K: 2.8 %, L: 2.8 %	cif fasta pdb
SOD1	8ccx	A, B	1.67 Å	X-RAY DIFFRACTION	A: 0.6 %, B: NA	cif fasta pdb
SOD1	8ccx	A, B	1.67 Å	X-RAY DIFFRACTION	A: 0.6 %, B: NA	cif fasta pdb
SOD1	8q6m	A, B	1.77 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %	cif fasta pdb
SOD1	5yto	A, B, C, D, E, F, G, H, I, J	1.90 Å	X-RAY DIFFRACTION	A: 13.9 %, B: 14.4 %, C: 14.4 %, D: 13.9 %, E: 14.4 %, F: 13.9 %, G: 15.0 %, H: 14.4 %, I: 15.0 %, J: 30.6 %	cif fasta pdb
SOD1	5ytu	A, B, C, D, E, F, G, H, I, J	1.90 Å	X-RAY DIFFRACTION	A: 14.4 %, B: 14.4 %, C: 14.4 %, D: 14.4 %, E: 13.9 %, F: 14.4 %, G: 30.6 %, H: 14.4 %, I: 15.6 %, J: 15.6 %	cif fasta pdb
SOD1	5yul	A, B, C, D, E, F, G, H, I, J	1.90 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: 0.6 %, G: NA, H: NA, I: NA, J: 18.2 %	cif fasta pdb
SOD1	7xx3	A, B, C, D, E, F, G, H, I, J	1.90 Å	X-RAY DIFFRACTION	A: 14.4 %, B: 14.4 %, C: 15.0 %, D: 14.4 %, E: 15.0 %, F: 15.0 %, G: 15.6 %, H: 14.4 %, I: 15.0 %, J: 30.0 %	cif fasta pdb
SOD1	8gsq	C	2.10 Å	X-RAY DIFFRACTION	C: NA	cif fasta pdb
SOD1	8gsq	A, B, D, F, I, J	2.10 Å	X-RAY DIFFRACTION	A: NA, B: NA, D: NA, F: NA, I: NA, J: NA	cif fasta pdb
SOD1	4b3e	A, B, C, D, E, F, G, H, I, J	2.15 Å	X-RAY DIFFRACTION	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %	cif fasta pdb
SOD1	6a9o	A, B, C, D, E, F, G, H, I, J	2.50 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: 17.5 %, H: 0.6 %, I: NA, J: NA	cif fasta pdb
SOD1	7fb9	A, B, C, D, E, F, G, H, I, J, K, L, M, N	2.70 Å	X-RAY DIFFRACTION	A: 5.0 %, B: 5.0 %, C: 5.6 %, D: 5.6 %, E: 5.0 %, F: 5.0 %, G: 5.0 %, H: 5.0 %, I: 5.0 %, J: 5.0 %, K: 5.0 %, L: 5.0 %, M: 57.8 %, N: 83.9 %	cif fasta pdb
SOD1	7vzf	A, B, C	2.95 Å	ELECTRON MICROSCOPY	A: 21.4 %, B: 21.4 %, C: 21.4 %	cif fasta pdb
SOD1	2c9v	A, B	1.07 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2c9v	A, B	1.07 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2v0a	A, B	1.15 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2v0a	A, B	1.15 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2c9s	A, B	1.24 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2c9s	A, B	1.24 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2c9u	A, B	1.24 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	2c9u	A, B	1.24 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	5o3y	A, B	1.30 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	5o3y	A, B	1.30 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	5o40	A, B	1.50 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	5o40	A, B	1.50 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	1pu0	A, B, C, D, E, F, G, H, I, J	1.70 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA	cif fasta pdb
SOD1	1hl5	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R	1.80 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: 1.3 %, F: 5.2 %, G: NA, H: NA, I: NA, J: NA, K: NA, L: 0.7 %, M: 0.7 %, N: NA, O: NA, P: NA, Q: NA, R: NA	cif fasta pdb
SOD1	1hl5	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R	1.80 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: 1.3 %, F: 5.2 %, G: NA, H: NA, I: NA, J: NA, K: NA, L: 0.7 %, M: 0.7 %, N: NA, O: NA, P: NA, Q: NA, R: NA	cif fasta pdb
SOD1	3t5w	A, B, C, D, E, F, G, H, I, J, K, L	1.80 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	cif fasta pdb
SOD1	3t5w	A, B, C, D, E, F, G, H, I, J, K, L	1.80 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	cif fasta pdb
SOD1	1hl4	A, B, C, D	1.82 Å	X-RAY DIFFRACTION	A: 0.6 %, B: NA, C: 17.5 %, D: 18.8 %	cif fasta pdb
SOD1	3ecu	A, B, C, D	1.90 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 17.6 %, D: 19.6 %	cif fasta pdb
SOD1	6ffk	A, B, C, D	1.94 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA	cif fasta pdb
SOD1	6ffk	A, B, C, D	1.94 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA	cif fasta pdb
SOD1	7nxx	A	2.19 Å	X-RAY DIFFRACTION	A: NA	cif fasta pdb
SOD1	3re0	A, B, C, D	2.28 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: 17.6 %, D: 19.6 %	cif fasta pdb
SOD1	1spd	A, B	2.40 Å	X-RAY DIFFRACTION	A: NA, B: NA	cif fasta pdb
SOD1	4ff9	A, B	2.50 Å	X-RAY DIFFRACTION	A: NA, B: 1.3 %	cif fasta pdb
SOD1	3kh3	A, B, C, D, E, F, G, H, I, J, K, L	3.50 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA, G: NA, H: NA, I: NA, J: NA, K: NA, L: NA	cif fasta pdb
SOD1	3kh4	A, B, C, D, E, F	3.50 Å	X-RAY DIFFRACTION	A: NA, B: NA, C: NA, D: NA, E: NA, F: NA	cif fasta pdb
SOD1	2nam	A	999.00 Å	SOLUTION NMR	A: 5.0 %	cif fasta pdb
SOD1	8gsq	H	2.10 Å	X-RAY DIFFRACTION	H: NA	cif fasta pdb

Gene	Uniprot ID	Protein name	AA	AlphaFold database	Download
PRPS1	P60891	Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) (PPRibP) (Phosphoribosyl pyrophosphate synthase I) (PRS-I)	318.0 Å	AlphaFold database	mmCif
SOD1	P00441	Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Superoxide dismutase 1) (hSod1)	154.0 Å	AlphaFold database	mmCif

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Residue numbering mismatch

The residue numbers in the PDB file and those in Uniprot differ for some chains
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Predicted model

This structure is from Swiss-Model. It is a computational model generated by threaded against a crystallised structure (Swissmodel docs ). It may be incorrect. E.g. missing ligands or broken cysteine bonds.

Engineered residues

The protein contains engineered residues () . Click this to make the residues in the structure to match Uniprot (irreversible):

Additional Infomation

Structure Info
PDB ID	8dbi
Structure name	Human PRPS1 with Phosphate, ATP, and R5P; Hexamer
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9
% unsolved residues	A: 2.8 %, B: 2.8 %, C: 2.8 %, D: 2.8 %, E: 2.8 %, F: 2.8 %
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	2h07
Structure name	crystal structure of human phosphoribosyl pyrophosphate synthetase 1 mutant S132A
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.22
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2006-05-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 21, B: 18
% unsolved residues	A: 6.4 %, B: 5.5 %
Unsolved residues	A: [MET1, PRO2, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	2h08
Structure name	crystal structure of human phosphoribosyl pyrophosphate synthetase 1 mutant Y146M
Resolution	2.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2006-05-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 21, B: 18
% unsolved residues	A: 6.4 %, B: 5.5 %
Unsolved residues	A: [MET1, PRO2, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	4f8e
Structure name	Crystal structure of human PRS1 D52H mutant
Resolution	2.27 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.18
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2012-05-17
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 18, B: 18
% unsolved residues	A: 5.5 %, B: 5.5 %
Unsolved residues	A: [MET1, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, ASP203, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	4lyg
Structure name	Crystal structure of human PRS1 E43T mutant
Resolution	3.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.3
R work	0.25
R observed	0.26
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2013-07-31
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 22, B: 16
% unsolved residues	A: 6.7 %, B: 4.9 %
Unsolved residues	A: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	4lzn
Structure name	Crystal structure of human PRS1 D65N mutant
Resolution	2.14 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.22
R observed	0.23
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2013-07-31
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 22, B: 18
% unsolved residues	A: 6.7 %, B: 5.5 %
Unsolved residues	A: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	4lzo
Structure name	Crystal structure of human PRS1 A87T mutant
Resolution	3.31 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.31
R work	0.26
R observed	0.27
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2013-07-31
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 22, B: 18
% unsolved residues	A: 6.7 %, B: 5.5 %
Unsolved residues	A: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	4m0p
Structure name	Crystal structure of human PRS1 M115T mutant
Resolution	2.11 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.17
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2013-08-01
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 22, B: 18
% unsolved residues	A: 6.7 %, B: 5.5 %
Unsolved residues	A: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	4m0u
Structure name	crystal structure of human PRS1 Q133P mutant
Resolution	2.74 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.3
R work	0.25
R observed	0.26
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2013-08-02
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 23, B: 18
% unsolved residues	A: 7.1 %, B: 5.5 %
Unsolved residues	A: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, PHE313, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, ASP203, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	8dbn
Structure name	Human PRPS1-E307A engineered mutation with Phosphate, ATP, and R5P; Hexamer
Resolution	2.40 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 14, B: 14, C: 14, D: 14, E: 14, F: 14
% unsolved residues	A: 4.4 %, B: 4.4 %, C: 4.4 %, D: 4.4 %, E: 4.4 %, F: 4.4 %
Unsolved residues	A: [SER1, GLY306, ALA307, SER308, VAL309, SER310, TYR311, LEU312, PHE313, SER314, HIS315, VAL316, PRO317, LEU318], B: [SER1, GLY306, ALA307, SER308, VAL309, SER310, TYR311, LEU312, PHE313, SER314, HIS315, VAL316, PRO317, LEU318], C: [SER1, GLY306, ALA307, SER308, VAL309, SER310, TYR311, LEU312, PHE313, SER314, HIS315, VAL316, PRO317, LEU318], D: [SER1, GLY306, ALA307, SER308, VAL309, SER310, TYR311, LEU312, PHE313, SER314, HIS315, VAL316, PRO317, LEU318], E: [SER1, GLY306, ALA307, SER308, VAL309, SER310, TYR311, LEU312, PHE313, SER314, HIS315, VAL316, PRO317, LEU318], F: [SER1, GLY306, ALA307, SER308, VAL309, SER310, TYR311, LEU312, PHE313, SER314, HIS315, VAL316, PRO317, LEU318]

Structure Info
PDB ID	1azv
Structure name	FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	1997-11-21
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	1mfm
Structure name	MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION
Resolution	1.02 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	0.12
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	1999-04-16
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	1dsw
Structure name	THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OF HUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAME CHARGE AS THE NATIVE PROTEIN
Resolution	999.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	SOLUTION NMR
Deposition date	2000-01-10
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	1fun
Structure name	SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)
Resolution	2.85 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	1998-07-23
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: []

Structure Info
PDB ID	2c9v
Structure name	Atomic resolution structure of Cu-Zn Human Superoxide dismutase
Resolution	1.07 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.16
R work	0.13
R observed	0.13
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	1sos
Structure name	ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE
Resolution	2.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	0.2
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	1992-02-11
Classification	OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: []

Structure Info
PDB ID	1n18
Structure name	Thermostable mutant of Human Superoxide Dismutase, C6A, C111S
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.22
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2002-10-16
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1, C: 1, D: 1, E: 1, F: 1, G: 1, H: 1, I: 1, J: 1
% unsolved residues	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %
Unsolved residues	A: [MET0], B: [MET0], C: [MET0], D: [MET0], E: [MET0], F: [MET0], G: [MET0], H: [MET0], I: [MET0], J: [MET0]

Structure Info
PDB ID	1n19
Structure name	Structure of the HSOD A4V mutant
Resolution	1.86 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2002-10-16
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1
% unsolved residues	A: 0.6 %, B: 0.6 %
Unsolved residues	A: [MET0], B: [MET0]

Structure Info
PDB ID	1oez
Structure name	Zn His46Arg mutant of Human Cu, Zn Superoxide Dismutase
Resolution	2.15 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-04-02
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan
Unsolved residues	A: [], B: [], C: [], D: []

Structure Info
PDB ID	1ozu
Structure name	Crystal Structure of Familial ALS Mutant S134N of human Cu,Zn Superoxide Dismutase (CuZnSOD) to 1.3A resolution
Resolution	1.30 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.18
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-04-09
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 3, B: 26
% unsolved residues	A: 2.0 %, B: 17.0 %
Unsolved residues	A: [GLU132, GLU133, ASN134], B: [LEU267, SER268, ARG269, LYS270, HIS271, GLY272, GLY273, PRO274, LYS275, ASP276, GLU277, GLU278, ARG279, LEU326, GLY327, LYS328, GLY329, GLY330, ASN331, GLU332, GLU333, ASN334, THR335, LYS336, THR337, GLY338]

Structure Info
PDB ID	1p1v
Structure name	Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant D125H to 1.4A
Resolution	1.40 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-04-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 7, B: 9, C: 7
% unsolved residues	A: 4.6 %, B: 5.9 %, C: 4.6 %
Unsolved residues	A: [GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135], B: [LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136], C: [GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135]

Structure Info
PDB ID	1ptz
Structure name	Crystal structure of the human CU, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (FALS) Mutant H43R
Resolution	1.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-06-23
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	4a7u
Structure name	Structure of human I113T SOD1 complexed with adrenaline in the p21 space group.
Resolution	0.98 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.15
R work	0.14
R observed	0.14
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-11-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	6z3v
Structure name	A4V mutant of human SOD1 bound with N-aryl benzoisoselenazolone derivative 13 in P21 space group
Resolution	1.25 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.18
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2020-05-22
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2gbt
Structure name	C6A/C111A CuZn Superoxide dismutase
Resolution	1.70 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2006-03-11
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1, C: 27, D: 29
% unsolved residues	A: 0.7 %, B: 0.7 %, C: 17.6 %, D: 19.0 %
Unsolved residues	A: [ALA1], B: [ALA1], C: [ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141], D: [ALA1, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	2gbu
Structure name	C6A/C111A/C57A/C146A apo CuZn Superoxide dismutase
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.22
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2006-03-11
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: 29, D: 30
% unsolved residues	A: nan, B: nan, C: 19.0 %, D: 19.6 %
Unsolved residues	A: [], B: [], C: [SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141], D: [ALA1, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	3k91
Structure name	Polysulfane Bridge in Cu-Zn Superoxide Dismutase
Resolution	1.75 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2009-10-15
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 5, B: 25
% unsolved residues	A: 3.3 %, B: 16.3 %
Unsolved residues	A: [GLU77, GLU78, GLY130, ASN131, GLU132], B: [SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138]

Structure Info
PDB ID	2r27
Structure name	Constitutively zinc-deficient mutant of human superoxide dismutase (SOD), C6A, H80S, H83S, C111S
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.18
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2007-08-24
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 20, B: 20
% unsolved residues	A: 13.0 %, B: 13.0 %
Unsolved residues	A: [MET0, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139], B: [MET0, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139]

Structure Info
PDB ID	2vr6
Structure name	Crystal Structure of G85R ALS mutant of Human Cu,Zn Superoxide Dismutase (CuZnSOD) at 1.3 A resolution
Resolution	1.30 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.18
R work	0.13
R observed	0.14
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2008-03-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	7t8g
Structure name	G93A mutant of human SOD1 bound with MR6-8-2 in P21 space group
Resolution	1.35 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.2
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2021-12-16
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2wyt
Structure name	1.0 A resolution structure of L38V SOD1 mutant
Resolution	1.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.15
R work	0.12
R observed	0.13
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2009-11-20
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2xjk
Structure name	Monomeric Human Cu,Zn Superoxide dismutase
Resolution	1.45 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.2
R work	0.17
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2010-07-07
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	2xjl
Structure name	Monomeric Human Cu,Zn Superoxide dismutase without Cu ligands
Resolution	1.55 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.18
R work	0.16
R observed	0.16
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2010-07-07
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	2zkw
Structure name	Crystal structure of human Cu-Zn superoxide dismutase mutant G85R in space group P21
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.19
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2008-03-31
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 10, B: 13
% unsolved residues	A: 6.3 %, B: 8.2 %
Unsolved residues	A: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0, ALA1, LYS23, GLU24, GLN153], B: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0, LYS23, GLU24, SER25, THR54, ALA55, GLY56, GLN153]

Structure Info
PDB ID	2zky
Structure name	Crystal structure of human Cu-Zn superoxide dismutase mutant G93A
Resolution	2.40 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.19
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2008-03-31
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 7, B: 7, C: 6, D: 6, E: 6, F: 6, G: 6, H: 6, I: 6, J: 6
% unsolved residues	A: 4.4 %, B: 4.4 %, C: 3.8 %, D: 3.8 %, E: 3.8 %, F: 3.8 %, G: 3.8 %, H: 3.8 %, I: 3.8 %, J: 3.8 %
Unsolved residues	A: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0, ALA1], B: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0, ALA1], C: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], D: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], E: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], F: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], G: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], H: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], I: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0], J: [GLY-5, PRO-4, LEU-3, GLY-2, SER-1, MET0]

Structure Info
PDB ID	3ecw
Structure name	Crystal structure of the ALS-related pathological mutant T54R of human apo Cu,Zn Superoxide Dismutase (SOD1)
Resolution	2.15 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.3
R work	0.2
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2008-09-02
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: 29, D: 30
% unsolved residues	A: nan, B: nan, C: 19.0 %, D: 19.6 %
Unsolved residues	A: [], B: [], C: [SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141], D: [LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	3gtv
Structure name	Human-mouse SOD1 chimera
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.18
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2009-03-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: [], K: [], L: []

Structure Info
PDB ID	3h2p
Structure name	Human SOD1 D124V Variant
Resolution	1.55 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.2
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2009-04-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 27, B: 24
% unsolved residues	A: 17.6 %, B: 15.7 %
Unsolved residues	A: [LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139], B: [ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138]

Structure Info
PDB ID	3qqd
Structure name	Human SOD1 H80R variant, P212121 crystal form
Resolution	1.65 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.18
R work	0.14
R observed	0.15
Polymer composition	heteromeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-02-15
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 31
% unsolved residues	A: 20.1 %
Unsolved residues	A: [ACE0, ALA1, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140]

Structure Info
PDB ID	3hff
Structure name	Monomeric human Cu,Zn Superoxide dismutase without Zn ligands
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.28
R work	0.22
R observed	0.23
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2009-05-11
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 38
% unsolved residues	A: 24.8 %
Unsolved residues	A: [GLU51, ASP52, ASN53, THR54, ALA55, GLY56, CYS57, THR58, SER59, ALA60, GLY61, PRO62, SER63, PHE64, ASN65, PRO66, LEU67, SER68, ARG69, LYS70, SER71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, SER80, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, GLN153]

Structure Info
PDB ID	3ltv
Structure name	Mouse-human sod1 chimera
Resolution	2.45 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2010-02-16
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: 3, D: 1, E: nan, F: nan
% unsolved residues	A: nan, B: nan, C: 2.0 %, D: 0.7 %, E: nan, F: nan
Unsolved residues	A: [], B: [], C: [LYS128, GLY129, GLY130], D: [GLN153], E: [], F: []

Structure Info
PDB ID	4a7g
Structure name	Structure of human I113T SOD1 mutant complexed with 4-methylpiperazin- 1-yl)quinazoline in the p21 space group.
Resolution	1.24 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.18
R work	0.14
R observed	0.14
Polymer composition	heteromeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-11-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	4bcy
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, mutation H43F
Resolution	1.27 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.2
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2012-10-03
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 7
% unsolved residues	A: 4.6 %
Unsolved residues	A: [ASN53, THR54, ALA55, GLY56, CYS57, THR58, SER59]

Structure Info
PDB ID	4bcz
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form.
Resolution	1.93 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.17
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2012-10-03
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: 1
% unsolved residues	A: nan, B: 0.9 %
Unsolved residues	A: [], B: [ALA1]

Structure Info
PDB ID	4bd4
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant H43F
Resolution	2.78 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.18
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2012-10-04
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1, C: 2, D: 6, E: 6, F: 8, G: 3, H: 10, I: 12
% unsolved residues	A: 0.9 %, B: 0.9 %, C: 1.8 %, D: 5.5 %, E: 5.5 %, F: 7.3 %, G: 2.7 %, H: 9.1 %, I: 10.9 %
Unsolved residues	A: [GLN110], B: [GLN110], C: [ALA1, GLN110], D: [ALA93, GLY94, ALA95, GLY96, ALA97, GLN110], E: [ASP62, ALA93, GLY94, ALA95, GLY96, GLN110], F: [ALA93, GLY94, ALA95, GLY96, ALA97, GLY98, SER99, GLN110], G: [ALA1, ALA109, GLN110], H: [GLU40, GLY41, LYS92, ALA93, GLY94, ALA95, GLY96, ALA97, GLY98, SER99], I: [GLY49, ALA50, GLY51, GLY52, LYS92, ALA93, GLY94, ALA95, GLY96, ALA97, GLY98, GLN110]

Structure Info
PDB ID	4mcm
Structure name	Human SOD1 C57S Mutant, As-isolated
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2013-08-21
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: 1, D: nan, E: 1, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
% unsolved residues	A: nan, B: nan, C: 0.7 %, D: nan, E: 0.7 %, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
Unsolved residues	A: [], B: [], C: [ALA1], D: [], E: [ALA1], F: [], G: [], H: [], I: [], J: [], K: [], L: []

Structure Info
PDB ID	4oh2
Structure name	Crystal Structure of Cu/Zn Superoxide Dismutase I149T
Resolution	2.38 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.16
R observed	0.16
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2014-01-16
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: []

Structure Info
PDB ID	4xcr
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant I35A
Resolution	3.60 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2014-12-18
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5j07
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P1/2
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2016-03-27
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5j0c
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P2/3
Resolution	1.60 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.14
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2016-03-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 2, B: nan
% unsolved residues	A: 1.8 %, B: nan
Unsolved residues	A: [MET0, SER113], B: []

Structure Info
PDB ID	5j0f
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P4/5
Resolution	1.25 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.17
R work	0.13
R observed	0.13
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2016-03-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5j0g
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P7/8
Resolution	2.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.18
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2016-03-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	A: nan, B: nan
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5k02
Structure name	Structure of human SOD1 with T2D mutation
Resolution	1.99 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.16
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2016-05-17
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan, M: nan, N: nan, O: nan, P: nan, Q: nan, R: nan, S: nan, T: nan, U: nan, V: nan, W: nan, X: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan, M: nan, N: nan, O: nan, P: nan, Q: nan, R: nan, S: nan, T: nan, U: nan, V: nan, W: nan, X: nan
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: [], K: [], L: [], M: [], N: [], O: [], P: [], Q: [], R: [], S: [], T: [], U: [], V: [], W: [], X: []

Structure Info
PDB ID	5u9m
Structure name	Copper-Zinc Superoxide Dismutase is Activated through a Sulfenic Acid Intermediate at a Copper-ion Entry Site
Resolution	2.35 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.19
R observed	0.19
Polymer composition	heteromeric protein
Oligomeric state	Hetero 2-mer
Symmetry	Asymmetric
Stoichometry	A1, B1
Structure method	X-RAY DIFFRACTION
Deposition date	2016-12-16
Classification	oxidoreductase/chaperone
Full validation report	access
N unsolved residues	B: 22, D: 14
% unsolved residues	B: 8.9 %, D: 5.6 %
Unsolved residues	B: [THR2, THR3, ASN4, ASP5, THR6, TYR7, PRO14, MET15, HIS16, ARG62, ASN63, CYS64, GLY65, LYS66, ASP242, ALA243, LEU244, ALA245, ASN246, ASN247, ILE248, LYS249], D: [THR2, THR3, ASN4, ASP5, MET15, HIS16, ASP242, ALA243, LEU244, ALA245, ASN246, ASN247, ILE248, LYS249]

Structure Info
PDB ID	6dtk
Structure name	Heterodimers of FALS mutant SOD enzyme
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.16
R observed	0.16
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2018-06-17
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 11, B: nan, C: nan, D: nan, E: nan
% unsolved residues	A: 3.4 %, B: nan, C: nan, D: nan, E: nan
Unsolved residues	A: [MET0, ALA156, ALA157, SER158, GLY159, GLY160, GLY161, GLY162, GLY163, SER164, GLY165], B: [], C: [], D: [], E: []

Structure Info
PDB ID	6flh
Structure name	Monomeric Human Cu,Zn Superoxide dismutase, SOD1 7+7, apo form
Resolution	1.79 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.2
R work	0.17
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2018-01-25
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	6foi
Structure name	Human Cys57/156Ala superoxide dismutase-1 (SOD1), as isolated.
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.22
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2018-02-07
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
% unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: [], K: [], L: []

Structure Info
PDB ID	6fol
Structure name	Domain II of the human copper chaperone in complex with human Cu,Zn superoxide dismutase
Resolution	2.55 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.21
R observed	0.21
Polymer composition	heteromeric protein
Oligomeric state	Hetero 2-mer
Symmetry	Asymmetric
Stoichometry	A1, B1
Structure method	X-RAY DIFFRACTION
Deposition date	2018-02-07
Classification	METAL BINDING PROTEIN
Full validation report	access
N unsolved residues	A: 2, D: 2, E: nan, H: 2
% unsolved residues	A: 1.3 %, D: 1.3 %, E: nan, H: 1.3 %
Unsolved residues	A: [GLY83, ALA84], D: [GLY83, ALA84], E: [], H: [GLY83, ALA84]

Structure Info
PDB ID	6fp6
Structure name	Complex of human Cu,Zn SOD1 with the human copper chaperone for SOD1 in a compact conformation
Resolution	3.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.19
R observed	0.19
Polymer composition	heteromeric protein
Oligomeric state	Hetero 2-mer
Symmetry	Asymmetric
Stoichometry	A1, B1
Structure method	X-RAY DIFFRACTION
Deposition date	2018-02-09
Classification	METAL BINDING PROTEIN
Full validation report	access
N unsolved residues	B: 43, D: 40, F: 40, H: 44, J: 42, L: 40, N: 40, P: 43, R: 42, T: 51, V: 128, X: 42
% unsolved residues	B: 15.7 %, D: 14.6 %, F: 14.6 %, H: 16.1 %, J: 15.3 %, L: 14.6 %, N: 14.6 %, P: 15.7 %, R: 15.3 %, T: 18.6 %, V: 46.7 %, X: 15.3 %
Unsolved residues	B: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, LEU83, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], D: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], F: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], H: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, GLN82, LEU83, GLN84, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], J: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], L: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], N: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, LEU46, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], P: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLY81, GLN82, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], R: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], T: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, MET20, THR21, ALA22, GLY68, THR69, GLY70, GLN82, LEU83, GLN84, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], V: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, GLY9, THR10, LEU11, ALA12, THR13, LEU14, GLU15, PHE16, ALA17, VAL18, GLN19, MET20, THR21, ALA22, GLN23, SER24, ALA25, VAL26, ASP27, ALA28, VAL29, ARG30, LYS31, SER32, LEU33, GLN34, GLY35, VAL36, ALA37, GLY38, VAL39, GLN40, ASP41, VAL42, GLU43, VAL44, HIS45, LEU46, GLU47, ASP48, GLN49, MET50, VAL51, LEU52, VAL53, HIS54, THR55, THR56, LEU57, PRO58, SER59, GLN60, GLU61, VAL62, GLN63, ALA64, LEU65, LEU66, GLU67, GLY68, THR69, GLY70, ARG71, GLN72, ALA73, VAL74, LEU75, LYS76, GLY77, MET78, GLY79, SER80, GLY81, GLN82, LEU83, GLN84, GLY94, GLY95, PRO96, GLY97, GLY235, LEU236, PHE237, GLN238, ASN239, PRO240, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274], X: [MET1, ALA2, SER3, ASP4, SER5, GLY6, ASN7, GLN8, LYS241, GLN242, ILE243, CYS244, SER245, CYS246, ASP247, GLY248, LEU249, THR250, ILE251, TRP252, GLU253, GLU254, ARG255, GLY256, ARG257, PRO258, ILE259, ALA260, GLY261, LYS262, GLY263, ARG264, LYS265, GLU266, SER267, ALA268, GLN269, PRO270, PRO271, ALA272, HIS273, LEU274]

Structure Info
PDB ID	6spi
Structure name	A4V MUTANT OF HUMAN SOD1 WITH EBSELEN DERIVATIVE 4
Resolution	2.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2019-09-01
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1, C: 1, D: 1, E: 1, F: 1, G: 1, H: 1, I: 1, J: 1, K: 1, L: 1
% unsolved residues	A: 0.6 %, B: 0.6 %, C: 0.6 %, D: 0.6 %, E: 0.6 %, F: 0.6 %, G: 0.6 %, H: 0.6 %, I: 0.6 %, J: 0.6 %, K: 0.6 %, L: 0.6 %
Unsolved residues	A: [MET0], B: [MET0], C: [MET0], D: [MET0], E: [MET0], F: [MET0], G: [MET0], H: [MET0], I: [MET0], J: [MET0], K: [MET0], L: [MET0]

Structure Info
PDB ID	7cjv
Structure name	Solution structure of monomeric superoxide dismutase 1 with an additional mutation H46W in a dilute environment
Resolution	999.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	SOLUTION NMR
Deposition date	2020-07-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	A: nan
Unsolved residues	A: []

Structure Info
PDB ID	7fb6
Structure name	C57D/C146D mutant of Human Cu, Zn Superoxide Dismutase (SOD1)
Resolution	1.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.18
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	X-RAY DIFFRACTION
Deposition date	2021-07-08
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 6, B: 17
% unsolved residues	A: 3.7 %, B: 10.6 %
Unsolved residues	A: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2], B: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0, ASP52, ASN53, THR54, ALA55, GLY56, ASP57, THR58, SER59, ALA60]

Structure Info
PDB ID	8gsq
Structure name	Structure based studies reveal an atypical antipsychotic drug candidate - Paliperidone as a potent hSOD1 modulator with implications in ALS treatment.
Resolution	2.10 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.17
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2022-09-06
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	E: nan, G: 21
% unsolved residues	E: nan, G: 13.6 %
Unsolved residues	E: [], G: [ALA0, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, ALA77, GLU78, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140]

Structure Info
PDB ID	3s5j
Structure name	2.0A Crystal structure of human phosphoribosyl pyrophosphate synthetase 1
Resolution	2.02 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.21
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-05-23
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 22, B: 18
% unsolved residues	NA
Unsolved residues	A: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	8dbe
Structure name	Human PRPS1 with ADP; Hexamer
Resolution	2.10 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 2, B: 2, C: 2, D: 2, E: 2, F: 2
% unsolved residues	NA
Unsolved residues	A: [MET1, LEU318], B: [MET1, LEU318], C: [MET1, LEU318], D: [MET1, LEU318], E: [MET1, LEU318], F: [MET1, LEU318]

Structure Info
PDB ID	2h06
Structure name	Crystal structure of human phosphoribosyl pyrophosphate synthetase 1
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2006-05-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 21, B: 18
% unsolved residues	NA
Unsolved residues	A: [MET1, PRO2, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	2hcr
Structure name	crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with AMP(ATP), cadmium and sulfate ion
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2006-06-18
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 21, B: 18
% unsolved residues	NA
Unsolved residues	A: [MET1, PRO2, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, SER314, HIS315, VAL316, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	3efh
Structure name	Crystal structure of human phosphoribosyl pyrophosphate synthetase 1
Resolution	2.60 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.22
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	X-RAY DIFFRACTION
Deposition date	2008-09-08
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 19, B: 19
% unsolved residues	NA
Unsolved residues	A: [MET1, PRO2, LYS198, ALA199, ASN200, GLU201, VAL202, ASP203, ARG204, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326], B: [MET1, PRO2, LYS198, ALA199, ASN200, GLU201, VAL202, ASP203, ARG204, PRO317, LEU318, LEU319, GLU320, HIS321, HIS322, HIS323, HIS324, HIS325, HIS326]

Structure Info
PDB ID	8dbc
Structure name	Human PRPS1 with Phosphate; Hexamer
Resolution	3.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9
% unsolved residues	NA
Unsolved residues	A: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbd
Structure name	Human PRPS1 with Phosphate; Filament Interface
Resolution	3.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 12-mer
Symmetry	Dihedral
Stoichometry	A12
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9, G: 9, H: 9, I: 9, J: 9, K: 9, L: 9
% unsolved residues	NA
Unsolved residues	A: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], G: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], H: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], I: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], J: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], K: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], L: [MET1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbi
Structure name	Human PRPS1 with Phosphate, ATP, and R5P; Hexamer
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbj
Structure name	Human PRPS1 with Phosphate, ATP, and R5P; Filament Interface
Resolution	2.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 12-mer
Symmetry	Dihedral
Stoichometry	A12
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9, G: 9, H: 9, I: 9, J: 9, K: 9, L: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], G: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], H: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], I: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], J: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], K: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], L: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbk
Structure name	Human PRPS1 with Phosphate, ATP, and R5P; Hexamer with resolved catalytic loops
Resolution	2.10 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 2, B: 2, C: 9, D: 9, E: 9, F: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, LEU318], B: [SER1, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbf
Structure name	Human PRPS1 with ADP; Filament Interface
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 12-mer
Symmetry	Dihedral
Stoichometry	A12
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 2, B: 2, C: 2, D: 2, E: 2, F: 2, G: 2, H: 2, I: 2, J: 2, K: 2, L: 2
% unsolved residues	NA
Unsolved residues	A: [SER1, LEU318], B: [SER1, LEU318], C: [SER1, LEU318], D: [SER1, LEU318], E: [SER1, LEU318], F: [SER1, LEU318], G: [SER1, LEU318], H: [SER1, LEU318], I: [SER1, LEU318], J: [SER1, LEU318], K: [SER1, LEU318], L: [SER1, LEU318]

Structure Info
PDB ID	8dbg
Structure name	Human PRPS1 with Phosphate and ATP; Hexamer
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbh
Structure name	Human PRPS1 with Phosphate and ATP; Filament Interface
Resolution	2.20 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 12-mer
Symmetry	Dihedral
Stoichometry	A12
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9, G: 9, H: 9, I: 9, J: 9, K: 9, L: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], G: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], H: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], I: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], J: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], K: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], L: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbl
Structure name	Human PRPS1 with Phosphate and PRPP; Hexamer
Resolution	2.40 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 6-mer
Symmetry	Dihedral
Stoichometry	A6
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8dbm
Structure name	Human PRPS1 with Phosphate and PRPP; Filament Interface
Resolution	2.40 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 12-mer
Symmetry	Dihedral
Stoichometry	A12
Structure method	ELECTRON MICROSCOPY
Deposition date	2022-06-14
Classification	TRANSFERASE
Full validation report	access
N unsolved residues	A: 9, B: 9, C: 9, D: 9, E: 9, F: 9, G: 9, H: 9, I: 9, J: 9, K: 9, L: 9
% unsolved residues	NA
Unsolved residues	A: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], B: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], C: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], D: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], E: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], F: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], G: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], H: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], I: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], J: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], K: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318], L: [SER1, ARG196, LYS197, LYS198, ALA199, ASN200, GLU201, VAL202, LEU318]

Structure Info
PDB ID	8ccx
Structure name	Human SOD1 in complex with S-XL6 cross-linker
Resolution	1.67 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.18
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2023-01-27
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: nan
% unsolved residues	NA
Unsolved residues	A: [MET0], B: []

Structure Info
PDB ID	8ccx
Structure name	Human SOD1 in complex with S-XL6 cross-linker
Resolution	1.67 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.18
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2023-01-27
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: nan
% unsolved residues	NA
Unsolved residues	A: [MET0], B: []

Structure Info
PDB ID	8q6m
Structure name	Human SOD1 low dose data collecton
Resolution	1.77 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.21
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2023-08-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1
% unsolved residues	NA
Unsolved residues	A: [MET0], B: [MET0]

Structure Info
PDB ID	5yto
Structure name	Crystal Structure of human Superoxide Dismutase I (hSOD1) in complex with a napthalene-catechol linked compound.
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.18
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-11-19
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 25, B: 26, C: 26, D: 25, E: 26, F: 25, G: 27, H: 26, I: 27, J: 55
% unsolved residues	NA
Unsolved residues	A: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2], B: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], C: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], D: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2], E: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], F: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2], G: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0], H: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], I: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0], J: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	5ytu
Structure name	Structure of human SOD1 complexed with isoproteranol in C2221 space group
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.18
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-11-20
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 26, B: 26, C: 26, D: 26, E: 25, F: 26, G: 55, H: 26, I: 28, J: 28
% unsolved residues	NA
Unsolved residues	A: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], B: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], C: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], D: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], E: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2], F: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], G: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141], H: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], I: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0, ALA1], J: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0, ALA1]

Structure Info
PDB ID	5yul
Structure name	Native Structure of hSOD1 in P6322 space group
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.19
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-11-22
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: 1, G: nan, H: nan, I: nan, J: 28
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [MET0], G: [], H: [], I: [], J: [MET0, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140]

Structure Info
PDB ID	7xx3
Structure name	Crystal structure of human Superoxide Dismutase (SOD1) in complex with a fungal metabolite molecule, Phialomustin B (PB)
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.23
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2022-05-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 26, B: 26, C: 27, D: 26, E: 27, F: 27, G: 28, H: 26, I: 27, J: 54
% unsolved residues	NA
Unsolved residues	A: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], B: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], C: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0], D: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], E: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0], F: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0], G: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0, ALA1], H: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1], I: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0], J: [MET-26, LYS-25, HIS-24, HIS-23, HIS-22, HIS-21, HIS-20, HIS-19, PRO-18, MET-17, SER-16, ASP-15, TYR-14, ASP-13, ILE-12, PRO-11, THR-10, THR-9, GLU-8, ASN-7, LEU-6, TYR-5, PHE-4, GLN-3, GLY-2, ALA-1, MET0, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	8gsq
Structure name	Structure based studies reveal an atypical antipsychotic drug candidate - Paliperidone as a potent hSOD1 modulator with implications in ALS treatment.
Resolution	2.10 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.17
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2022-09-06
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	C: nan
% unsolved residues	NA
Unsolved residues	C: []

Structure Info
PDB ID	8gsq
Structure name	Structure based studies reveal an atypical antipsychotic drug candidate - Paliperidone as a potent hSOD1 modulator with implications in ALS treatment.
Resolution	2.10 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.17
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2022-09-06
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, D: nan, F: nan, I: nan, J: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], D: [], F: [], I: [], J: []

Structure Info
PDB ID	4b3e
Structure name	Structure of copper-zinc superoxide dismutase complexed with bicarbonate.
Resolution	2.15 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.17
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2012-07-23
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: 1, C: 1, D: 1, E: 1, F: 1, G: 1, H: 1, I: 1, J: 1
% unsolved residues	NA
Unsolved residues	A: [MET0], B: [MET0], C: [MET0], D: [MET0], E: [MET0], F: [MET0], G: [MET0], H: [MET0], I: [MET0], J: [MET0]

Structure Info
PDB ID	6a9o
Structure name	Rational discovery of a SOD1 tryptophan oxidation inhibitor with therapeutic potential for amyotrophic lateral sclerosis
Resolution	2.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.16
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2018-07-14
Classification	OXIDOREDUCTASE/INHIBITOR
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: 27, H: 1, I: nan, J: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [MET0, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140], H: [MET0], I: [], J: []

Structure Info
PDB ID	7fb9
Structure name	Crystal Structure of Human Cu, Zn Superoxide Dismutase (SOD1)
Resolution	2.70 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.23
R observed	0.23
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2021-07-08
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 8, B: 8, C: 9, D: 9, E: 8, F: 8, G: 8, H: 8, I: 8, J: 8, K: 8, L: 8, M: 93, N: 135
% unsolved residues	NA
Unsolved residues	A: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], B: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], C: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0, ALA1], D: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0, ALA1], E: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], F: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], G: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], H: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], I: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], J: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], K: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], L: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0], M: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0, ALA1, THR2, LYS3, ALA4, VAL5, CYS6, VAL7, LEU8, LYS9, GLY10, ASP11, GLY12, PRO13, VAL14, GLN15, GLY16, ILE17, ILE18, ASN19, PHE20, GLU21, GLN22, LYS23, GLU24, SER25, ASN26, GLY27, PRO28, VAL29, LYS30, VAL31, TRP32, GLY33, SER34, ILE35, LYS36, GLY37, LEU38, THR39, GLU40, GLY41, LEU42, HIS43, GLY44, PHE45, PHE50, GLY51, ASP52, ASN53, THR54, GLY85, ASN86, VAL87, THR88, ALA89, ASP90, LYS91, ASP92, GLY93, VAL94, ALA95, ASP96, VAL97, SER98, ILE99, GLU100, ASP101, SER102, VAL103, ILE104, SER105, LEU106, SER107, GLY108, ASP109, HIS110, CYS111, ILE112, ILE113, GLY114, ILE149, GLY150, ILE151, ALA152, GLN153], N: [GLY-7, ALA-6, MET-5, ASP-4, PRO-3, GLU-2, PHE-1, MET0, ALA1, THR2, LYS3, ALA4, VAL5, CYS6, VAL7, LEU8, LYS9, GLY10, ASP11, GLY12, PRO13, VAL14, GLN15, GLY16, ILE17, ILE18, ASN19, PHE20, GLU21, GLN22, LYS23, GLU24, SER25, ASN26, GLY27, PRO28, VAL29, LYS30, VAL31, TRP32, GLY33, SER34, ILE35, LYS36, GLY37, LEU38, THR39, GLU40, GLY41, LEU42, HIS43, GLY44, PHE45, HIS46, VAL47, HIS48, GLU49, PHE50, GLY51, ASP52, ASN53, THR54, ALA55, GLY56, CYS57, THR58, SER59, ALA60, GLY61, PRO62, HIS63, PHE64, ASN65, PRO66, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, VAL87, THR88, ALA89, ASP90, LYS91, ASP92, GLY93, VAL94, ALA95, ASP96, VAL97, SER98, ILE99, GLU100, ASP101, SER102, VAL103, ILE104, SER105, LEU106, SER107, GLY108, ASP109, HIS110, CYS111, ILE112, ILE113, GLY114, ARG115, THR116, LEU117, VAL118, VAL119, HIS120, GLU121, LYS122, ALA123, ASP124, ASP125, ALA140, GLY141, SER142, ARG143, LEU144, ALA145, CYS146, GLY147, VAL148, ILE149, GLY150, ILE151, ALA152, GLN153]

Structure Info
PDB ID	7vzf
Structure name	Cryo-EM structure of amyloid fibril formed by full-length human SOD1
Resolution	2.95 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Homo 3-mer
Symmetry	Asymmetric
Stoichometry	A3
Structure method	ELECTRON MICROSCOPY
Deposition date	2021-11-16
Classification	PROTEIN FIBRIL
Full validation report	access
N unsolved residues	A: 33, B: 33, C: 33
% unsolved residues	NA
Unsolved residues	A: [MET0, ALA1, THR2, GLY56, CYS57, THR58, SER59, ALA60, GLY61, PRO62, HIS63, PHE64, ASN65, PRO66, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, HIS80, VAL81, GLY82, ASP83, LEU84, GLY85], B: [MET0, ALA1, THR2, GLY56, CYS57, THR58, SER59, ALA60, GLY61, PRO62, HIS63, PHE64, ASN65, PRO66, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, HIS80, VAL81, GLY82, ASP83, LEU84, GLY85], C: [MET0, ALA1, THR2, GLY56, CYS57, THR58, SER59, ALA60, GLY61, PRO62, HIS63, PHE64, ASN65, PRO66, LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, HIS80, VAL81, GLY82, ASP83, LEU84, GLY85]

Structure Info
PDB ID	2c9v
Structure name	Atomic resolution structure of Cu-Zn Human Superoxide dismutase
Resolution	1.07 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.16
R work	0.13
R observed	0.13
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2c9v
Structure name	Atomic resolution structure of Cu-Zn Human Superoxide dismutase
Resolution	1.07 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.16
R work	0.13
R observed	0.13
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2v0a
Structure name	Atomic resolution crystal structure of Human Superoxide Dismutase
Resolution	1.15 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.15
R observed	0.16
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2007-05-11
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2v0a
Structure name	Atomic resolution crystal structure of Human Superoxide Dismutase
Resolution	1.15 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.15
R observed	0.16
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2007-05-11
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2c9s
Structure name	1.24 Angstroms resolution structure of Zn-Zn Human Superoxide dismutase
Resolution	1.24 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2c9s
Structure name	1.24 Angstroms resolution structure of Zn-Zn Human Superoxide dismutase
Resolution	1.24 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2c9u
Structure name	1.24 Angstroms resolution structure of as-isolated Cu-Zn Human Superoxide dismutase
Resolution	1.24 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.18
R work	0.14
R observed	0.14
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	2c9u
Structure name	1.24 Angstroms resolution structure of as-isolated Cu-Zn Human Superoxide dismutase
Resolution	1.24 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.18
R work	0.14
R observed	0.14
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2005-12-14
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5o3y
Structure name	SOD1 bound to Ebsulfur
Resolution	1.30 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-05-25
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5o3y
Structure name	SOD1 bound to Ebsulfur
Resolution	1.30 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.19
R work	0.15
R observed	0.15
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-05-25
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5o40
Structure name	SOD1 bound to Ebselen
Resolution	1.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.17
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-05-25
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	5o40
Structure name	SOD1 bound to Ebselen
Resolution	1.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.17
R observed	0.17
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2017-05-25
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	1pu0
Structure name	Structure of Human Cu,Zn Superoxide Dismutase
Resolution	1.70 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.21
R observed	0.21
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-06-23
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: []

Structure Info
PDB ID	1hl5
Structure name	The Structure of Holo Type Human Cu, Zn Superoxide Dismutase
Resolution	1.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.18
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-03-13
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: 2, F: 8, G: nan, H: nan, I: nan, J: nan, K: nan, L: 1, M: 1, N: nan, O: nan, P: nan, Q: nan, R: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [GLY108, ASP109], F: [ALA1, THR2, GLN22, LYS23, GLU24, SER25, ASN26, GLY27], G: [], H: [], I: [], J: [], K: [], L: [ALA1], M: [ALA1], N: [], O: [], P: [], Q: [], R: []

Structure Info
PDB ID	1hl5
Structure name	The Structure of Holo Type Human Cu, Zn Superoxide Dismutase
Resolution	1.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.22
R work	0.18
R observed	0.19
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-03-13
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: 2, F: 8, G: nan, H: nan, I: nan, J: nan, K: nan, L: 1, M: 1, N: nan, O: nan, P: nan, Q: nan, R: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [GLY108, ASP109], F: [ALA1, THR2, GLN22, LYS23, GLU24, SER25, ASN26, GLY27], G: [], H: [], I: [], J: [], K: [], L: [ALA1], M: [ALA1], N: [], O: [], P: [], Q: [], R: []

Structure Info
PDB ID	3t5w
Structure name	2ME modified human SOD1
Resolution	1.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-07-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: [], K: [], L: []

Structure Info
PDB ID	3t5w
Structure name	2ME modified human SOD1
Resolution	1.80 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.24
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-07-28
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: [], K: [], L: []

Structure Info
PDB ID	1hl4
Structure name	The Structure of Apo Type Human Cu, Zn Superoxide Dismutase
Resolution	1.82 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.28
R work	0.23
R observed	0.23
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2003-03-13
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: 1, B: nan, C: 27, D: 29
% unsolved residues	NA
Unsolved residues	A: [ACE0], B: [], C: [ACE0, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140], D: [ACE0, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	3ecu
Structure name	Crystal structure of human apo Cu,Zn Superoxide Dismutase (SOD1)
Resolution	1.90 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.28
R work	0.24
R observed	0.24
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2008-09-02
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: 27, D: 30
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140], D: [LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	6ffk
Structure name	Human apo-SOD1 bound to PtCl2(1R,2R-1,4-DACH
Resolution	1.94 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.23
R observed	0.23
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2018-01-08
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: []

Structure Info
PDB ID	6ffk
Structure name	Human apo-SOD1 bound to PtCl2(1R,2R-1,4-DACH
Resolution	1.94 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.26
R work	0.23
R observed	0.23
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2018-01-08
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: []

Structure Info
PDB ID	7nxx
Structure name	Structure of Superoxide Dismutase 1 (SOD1) in complex with nanobody 2 (Nb2).
Resolution	2.19 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.25
R work	0.2
R observed	0.2
Polymer composition	heteromeric protein
Oligomeric state	Hetero 4-mer
Symmetry	Cyclic
Stoichometry	A2, B2
Structure method	X-RAY DIFFRACTION
Deposition date	2021-03-19
Classification	METAL BINDING PROTEIN
Full validation report	access
N unsolved residues	A: nan
% unsolved residues	NA
Unsolved residues	A: []

Structure Info
PDB ID	3re0
Structure name	Crystal structure of human apo Cu,Zn superoxide dismutase (SOD1) complexed with cisplatin
Resolution	2.28 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.29
R work	0.21
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2011-04-02
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: 27, D: 30
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140], D: [LEU67, SER68, ARG69, LYS70, HIS71, GLY72, GLY73, PRO74, LYS75, ASP76, GLU77, GLU78, ARG79, ASP125, LEU126, GLY127, LYS128, GLY129, GLY130, ASN131, GLU132, GLU133, SER134, THR135, LYS136, THR137, GLY138, ASN139, ALA140, GLY141]

Structure Info
PDB ID	1spd
Structure name	AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE
Resolution	2.40 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	0.22
R observed	0.22
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	1993-07-21
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan
% unsolved residues	NA
Unsolved residues	A: [], B: []

Structure Info
PDB ID	4ff9
Structure name	Crystal Structure of cysteinylated WT SOD1.
Resolution	2.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.34
R work	0.28
R observed	0.28
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2012-05-31
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: 2
% unsolved residues	NA
Unsolved residues	A: [], B: [GLU24, SER25]

Structure Info
PDB ID	3kh3
Structure name	Crystal structure of human Cu/Zn superoxide dismutase recombinantly produced in Leishmania tarantolae; P212121 crystal form containing 12 chains in the asymmetric unit
Resolution	3.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.28
R work	0.24
R observed	0.24
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2009-10-30
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan, G: nan, H: nan, I: nan, J: nan, K: nan, L: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: [], G: [], H: [], I: [], J: [], K: [], L: []

Structure Info
PDB ID	3kh4
Structure name	Crystal structure of human Cu/Zn superoxide dismutase recombinantly produced in Leishmania tarantolae; P6522 crystal form containing 6 chains in the asymmetric unit
Resolution	3.50 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.2
R observed	0.2
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2009-10-30
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	A: nan, B: nan, C: nan, D: nan, E: nan, F: nan
% unsolved residues	NA
Unsolved residues	A: [], B: [], C: [], D: [], E: [], F: []

Structure Info
PDB ID	2nam
Structure name	Full-length WT SOD1 in DPC MICELLE
Resolution	999.00 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	NA
R work	NA
R observed	NA
Polymer composition	homomeric protein
Oligomeric state	Monomer
Symmetry	Asymmetric
Stoichometry	A1
Structure method	SOLUTION NMR
Deposition date	2016-01-06
Classification	METAL BINDING PROTEIN
Full validation report	access
N unsolved residues	A: 8
% unsolved residues	NA
Unsolved residues	A: [MET-7, GLY-6, HIS-5, HIS-4, HIS-3, HIS-2, HIS-1, HIS0]

Structure Info
PDB ID	8gsq
Structure name	Structure based studies reveal an atypical antipsychotic drug candidate - Paliperidone as a potent hSOD1 modulator with implications in ALS treatment.
Resolution	2.10 Å
VCF variant	NA
Mutation from VCF variant	NA
R free	0.21
R work	0.17
R observed	0.18
Polymer composition	homomeric protein
Oligomeric state	Homo 2-mer
Symmetry	Cyclic
Stoichometry	A2
Structure method	X-RAY DIFFRACTION
Deposition date	2022-09-06
Classification	OXIDOREDUCTASE
Full validation report	access
N unsolved residues	H: nan
% unsolved residues	NA
Unsolved residues	H: []

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Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1681.0
Bit	652.129
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1681.0
Bit	652.129
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	VCV000009930
Title	NM_002764.4(PRPS1):c.154G>C (p.Asp52His)
Variant type	single nucleotide variant
Protein change	D52H
Aliases	NA
Clinical significance	Pathogenic
Last evaluated	1975/11/01 00:00
Review status	no assertion criteria provided
Associated traits	Phosphoribosylpyrophosphate synthetase superactivity
dbs_and_accessions	['Orphanet: 3222', 'MedGen: C1970827', 'MONDO: MONDO:0010395', 'OMIM: 300661']

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1683.0
Bit	652.899
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	VCV000009938
Title	NM_002764.4(PRPS1):c.193G>A (p.Asp65Asn)
Variant type	single nucleotide variant
Protein change	D65N
Aliases	NA
Clinical significance	Pathogenic
Last evaluated	2010/01/01 00:00
Review status	no assertion criteria provided
Associated traits	Hearing loss, X-linked 1
dbs_and_accessions	['Orphanet: 90625', 'MedGen: C1844677', 'MONDO: MONDO:0010577', 'OMIM: 304500']

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	VCV000009939
Title	NM_002764.4(PRPS1):c.259G>A (p.Ala87Thr)
Variant type	single nucleotide variant
Protein change	A87T
Aliases	NA
Clinical significance	Uncertain significance
Last evaluated	2021/08/30 00:00
Review status	criteria provided, single submitter
Associated traits	Charcot-Marie-Tooth Neuropathy X
dbs_and_accessions	['MedGen: CN118851']

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1681.0
Bit	652.129
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	VCV000009935
Title	NM_002764.4(PRPS1):c.344T>C (p.Met115Thr)
Variant type	single nucleotide variant
Protein change	M115T
Aliases	NA
Clinical significance	Likely pathogenic
Last evaluated	2021/07/14 00:00
Review status	criteria provided, single submitter
Associated traits	Charcot-Marie-Tooth Neuropathy X
dbs_and_accessions	['MedGen: CN118851']

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1680.0
Bit	651.744
e-value	0.0
Similarity	0.9968553459119496
Gaps	0.0

ClinVar Info
Accession	VCV000009937
Title	NM_002764.4(PRPS1):c.398A>C (p.Gln133Pro)
Variant type	single nucleotide variant
Protein change	Q133P
Aliases	NA
Clinical significance	Pathogenic
Last evaluated	2007/09/01 00:00
Review status	no assertion criteria provided
Associated traits	Arts syndrome
dbs_and_accessions	['Orphanet: 1187', 'MedGen: C0796028', 'MONDO: MONDO:0010533', 'OMIM: 301835']

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	317.0
Score	1678.0
Bit	650.9730000000002
e-value	0.0
Similarity	0.9968454258675079
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	779.0
Bit	304.6790000000001
e-value	3.56314999999996e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014752
Title	NM_000454.5(SOD1):c.112G>A (p.Gly38Arg)
Variant type	single nucleotide variant
Protein change	G38R
Aliases	G37R
Clinical significance	Pathogenic
Last evaluated	2016/08/31 00:00
Review status	criteria provided, single submitter
Associated traits	Motor neuron disease
dbs_and_accessions	['Orphanet: 98503', 'MedGen: C0085084', 'MONDO: MONDO:0020128']

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	754.0
Bit	295.0490000000001
e-value	2.6704799999999996e-109
Similarity	0.9673202614379084
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	744.0
Bit	291.197
e-value	8.751049999999985e-108
Similarity	0.9607843137254902
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	153.0
Score	769.0
Bit	300.827
e-value	1.3922799999999999e-111
Similarity	0.9803921568627452
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	153.0
Score	772.0
Bit	301.982
e-value	3.929759999999968e-112
Similarity	0.9869281045751634
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	780.0
Bit	305.064
e-value	2.6129499999999836e-113
Similarity	0.987012987012987
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	775.0
Bit	303.138
e-value	1.546139999999984e-112
Similarity	0.9805194805194806
Gaps	0.0

ClinVar Info
Accession	VCV000014763
Title	NM_000454.5(SOD1):c.14C>T (p.Ala5Val)
Variant type	single nucleotide variant
Protein change	A5V
Aliases	A4V
Clinical significance	Pathogenic
Last evaluated	2021/12/18 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	Amyotrophic lateral sclerosis type 1, not provided
dbs_and_accessions	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	780.0
Bit	305.064
e-value	2.6786199999999956e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014764
Title	NM_000454.5(SOD1):c.140A>G (p.His47Arg)
Variant type	single nucleotide variant
Protein change	H47R
Aliases	H46R
Clinical significance	Pathogenic
Last evaluated	2022/01/01 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	Amyotrophic lateral sclerosis type 1, not provided, Amyotrophic lateral sclerosis
dbs_and_accessions	['Orphanet: 803', 'MedGen: C0002736', 'MONDO: MONDO:0004976', 'OMIM: 105400', 'Human Phenotype Ontology: HP:0007354']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	782.0
Bit	305.834
e-value	1.2981899999998751e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014774
Title	NM_000454.5(SOD1):c.404G>A (p.Ser135Asn)
Variant type	single nucleotide variant
Protein change	S135N
Aliases	S134N
Clinical significance	Pathogenic
Last evaluated	1997/01/01 00:00
Review status	no assertion criteria provided
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B, C
Alignment length	154.0
HSP length	153.0
Score	778.0
Bit	304.2940000000001
e-value	4.68802999999991e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	766.0
Bit	299.671
e-value	3.4240599999999946e-111
Similarity	0.9803921568627452
Gaps	0.0

ClinVar Info
Accession	VCV000014756
Title	NM_000454.5(SOD1):c.131A>G (p.His44Arg)
Variant type	single nucleotide variant
Protein change	H44R
Aliases	H43R
Clinical significance	Pathogenic
Last evaluated	2021/11/17 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	not provided, Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	782.0
Bit	305.834
e-value	1.2154599999998824e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014762
Title	NM_000454.5(SOD1):c.338T>C (p.Ile113Thr)
Variant type	single nucleotide variant
Protein change	I113T
Aliases	NA
Clinical significance	Pathogenic
Last evaluated	2021/09/17 00:00
Review status	criteria provided, single submitter
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	781.0
Bit	305.449
e-value	1.70801999999998e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014763
Title	NM_000454.5(SOD1):c.14C>T (p.Ala5Val)
Variant type	single nucleotide variant
Protein change	A5V
Aliases	A4V
Clinical significance	Pathogenic
Last evaluated	2021/12/18 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	Amyotrophic lateral sclerosis type 1, not provided
dbs_and_accessions	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	772.0
Bit	301.982
e-value	3.454899999999995e-112
Similarity	0.9869281045751634
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	764.0
Bit	298.901
e-value	7.14268e-111
Similarity	0.9738562091503268
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	774.0
Bit	302.753
e-value	1.788409999999945e-112
Similarity	0.9869281045751634
Gaps	0.0

ClinVar Info
Accession	VCV000014764
Title	NM_000454.5(SOD1):c.140A>G (p.His47Arg)
Variant type	single nucleotide variant
Protein change	H47R
Aliases	H46R
Clinical significance	Pathogenic
Last evaluated	2022/01/01 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	Amyotrophic lateral sclerosis type 1, not provided, Amyotrophic lateral sclerosis
dbs_and_accessions	['Orphanet: 803', 'MedGen: C0002736', 'MONDO: MONDO:0004976', 'OMIM: 105400', 'Human Phenotype Ontology: HP:0007354']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	768.0
Bit	300.442
e-value	1.5492399999999961e-111
Similarity	0.9740259740259741
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	779.0
Bit	304.6790000000001
e-value	3.56314999999996e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014758
Title	NM_000454.5(SOD1):c.256G>C (p.Gly86Arg)
Variant type	single nucleotide variant
Protein change	G86R
Aliases	G85R
Clinical significance	Likely pathogenic
Last evaluated	2021/09/17 00:00
Review status	criteria provided, single submitter
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	782.0
Bit	305.834
e-value	1.2561399999999787e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014760
Title	NM_000454.5(SOD1):c.281G>C (p.Gly94Ala)
Variant type	single nucleotide variant
Protein change	G94A
Aliases	G93A
Clinical significance	Pathogenic
Last evaluated	1997/07/25 00:00
Review status	no assertion criteria provided
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	783.0
Bit	306.22
e-value	9.866859999998993e-114
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014753
Title	NM_000454.5(SOD1):c.115C>G (p.Leu39Val)
Variant type	single nucleotide variant
Protein change	L39V
Aliases	L38V
Clinical significance	Likely pathogenic
Last evaluated	2021/08/14 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	not provided, Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['MedGen: C1862939', 'Orphanet: 803', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	757.0
Bit	296.204
e-value	8.530019999999996e-110
Similarity	0.9738562091503268
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	738.0
Bit	288.88599999999997
e-value	7.354579999999994e-107
Similarity	0.954248366013072
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	786.0
Bit	307.375
e-value	4.2568399999998386e-114
Similarity	0.9935064935064936
Gaps	0.0

ClinVar Info
Accession	VCV000014758
Title	NM_000454.5(SOD1):c.256G>C (p.Gly86Arg)
Variant type	single nucleotide variant
Protein change	G86R
Aliases	G85R
Clinical significance	Likely pathogenic
Last evaluated	2021/09/17 00:00
Review status	criteria provided, single submitter
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	789.0
Bit	308.531
e-value	1.5681199999998537e-114
Similarity	0.9935064935064936
Gaps	0.0

ClinVar Info
Accession	VCV000014760
Title	NM_000454.5(SOD1):c.281G>C (p.Gly94Ala)
Variant type	single nucleotide variant
Protein change	G94A
Aliases	G93A
Clinical significance	Pathogenic
Last evaluated	1997/07/25 00:00
Review status	no assertion criteria provided
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	780.0
Bit	305.064
e-value	2.5635799999997784e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	153.0
Score	752.0
Bit	294.278
e-value	4.6224899999999915e-109
Similarity	0.954248366013072
Gaps	0.0

ClinVar Info
Accession	VCV000014783
Title	NM_000454.5(SOD1):c.289G>A (p.Asp97Asn)
Variant type	single nucleotide variant
Protein change	D97N
Aliases	D96N
Clinical significance	Uncertain significance
Last evaluated	2018/11/20 00:00
Review status	criteria provided, single submitter
Associated traits	not provided
dbs_and_accessions	['MedGen: CN517202']

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	777.0
Bit	303.908
e-value	7.03623999999992e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	780.0
Bit	305.064
e-value	2.79079999999997e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	VCV000014782
Title	NM_000454.5(SOD1):c.242A>G (p.His81Arg)
Variant type	single nucleotide variant
Protein change	H81R
Aliases	H80R
Clinical significance	Pathogenic
Last evaluated	2021/08/24 00:00
Review status	criteria provided, single submitter
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	732.0
Bit	286.574
e-value	5.185439999999993e-106
Similarity	0.9477124183006536
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	154.0
HSP length	153.0
Score	690.0
Bit	270.39599999999996
e-value	1.21688e-99
Similarity	0.8823529411764706
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	777.0
Bit	303.908
e-value	7.5151499999999e-113
Similarity	0.9869281045751634
Gaps	0.0

ClinVar Info
Accession	VCV000014762
Title	NM_000454.5(SOD1):c.338T>C (p.Ile113Thr)
Variant type	single nucleotide variant
Protein change	I113T
Aliases	NA
Clinical significance	Pathogenic
Last evaluated	2021/09/17 00:00
Review status	criteria provided, single submitter
Associated traits	Amyotrophic lateral sclerosis type 1
dbs_and_accessions	['Orphanet: 803', 'MedGen: C1862939', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	750.0
Bit	293.508
e-value	1.0760499999999964e-108
Similarity	0.9673202614379084
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	437.0
Bit	172.94
e-value	8.021039999999996e-62
Similarity	0.6797385620915033
Gaps	43.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I
Alignment length	154.0
HSP length	153.0
Score	430.0
Bit	170.24400000000003
e-value	9.637669999999995e-61
Similarity	0.673202614379085
Gaps	43.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	153.0
Score	778.0
Bit	304.2940000000001
e-value	4.79206999999991e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	153.0
Score	768.0
Bit	300.442
e-value	1.9780699999999996e-111
Similarity	0.9803921568627452
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	432.0
Bit	171.014
e-value	4.4773999999999964e-61
Similarity	0.673202614379085
Gaps	43.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	141.0
Score	389.0
Bit	154.451
e-value	2.3196e-54
Similarity	0.6595744680851063
Gaps	43.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	126.0
Score	307.0
Bit	122.865
e-value	5.605579999999999e-42
Similarity	0.6190476190476191
Gaps	43.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	48.0
Score	250.0
Bit	100.90799999999999
e-value	2.2021199999999997e-33
Similarity	0.9791666666666666
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	123.0
Score	406.0
Bit	160.999
e-value	4.82562e-57
Similarity	0.7235772357723578
Gaps	30.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Alignment length	154.0
HSP length	153.0
Score	779.0
Bit	304.6790000000001
e-value	3.26364999999997e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	B, D
Alignment length	154.0
HSP length	29.0
Score	32.0
Bit	16.9346
e-value	0.221833
Similarity	0.3448275862068966
Gaps	1.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E
Alignment length	154.0
HSP length	154.0
Score	781.0
Bit	305.449
e-value	1.2219599999999986e-110
Similarity	0.987012987012987
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	481.0
Bit	189.889
e-value	2.4475299999999982e-68
Similarity	0.7385620915032679
Gaps	35.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	153.0
Score	772.0
Bit	301.982
e-value	3.454899999999995e-112
Similarity	0.9869281045751634
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, D, E, H
Alignment length	154.0
HSP length	146.0
Score	341.0
Bit	135.961
e-value	1.2343099999999999e-46
Similarity	0.5
Gaps	4.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	B, D, F, H, J, L, N, P, R, T, V, X
Alignment length	154.0
HSP length	146.0
Score	346.0
Bit	137.887
e-value	1.5876e-45
Similarity	0.5
Gaps	4.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	154.0
Score	788.0
Bit	308.145
e-value	1.644479999999983e-114
Similarity	0.9935064935064936
Gaps	0.0

ClinVar Info
Accession	VCV000014763
Title	NM_000454.5(SOD1):c.14C>T (p.Ala5Val)
Variant type	single nucleotide variant
Protein change	A5V
Aliases	A4V
Clinical significance	Pathogenic
Last evaluated	2021/12/18 00:00
Review status	criteria provided, multiple submitters, no conflicts
Associated traits	Amyotrophic lateral sclerosis type 1, not provided
dbs_and_accessions	['Orphanet: 803', 'MedGen: CN517202', 'MONDO: MONDO:0007103', 'OMIM: 105400']

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	429.0
Bit	169.859
e-value	1.2534899999999982e-60
Similarity	0.673202614379085
Gaps	43.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	772.0
Bit	301.982
e-value	5.967489999999991e-112
Similarity	0.987012987012987
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	E, G
Alignment length	154.0
HSP length	153.0
Score	782.0
Bit	305.834
e-value	1.4605699999999904e-113
Similarity	0.9934640522875816
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1688.0
Bit	654.825
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	318.0
Score	1690.0
Bit	655.596
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1688.0
Bit	654.825
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1688.0
Bit	654.825
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	318.0
HSP length	318.0
Score	1688.0
Bit	654.825
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	318.0
Score	1690.0
Bit	655.596
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	318.0
HSP length	318.0
Score	1690.0
Bit	655.596
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	318.0
HSP length	317.0
Score	1684.0
Bit	653.284
e-value	0.0
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.071
e-value	3.033909999999984e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.071
e-value	3.033909999999984e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.071
e-value	3.033909999999984e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	795.0
Bit	310.842
e-value	4.42527e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	795.0
Bit	310.842
e-value	4.42527e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.07099999999997
e-value	3.0339099999997105e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	795.0
Bit	310.842
e-value	4.42527e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	C
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.071
e-value	2.3503899999999957e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, D, F, I, J
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.071
e-value	3.033909999999979e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.07099999999997
e-value	3.0339099999997105e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.07099999999997
e-value	3.0339099999997105e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L, M, N
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.07099999999997
e-value	3.5818799999999836e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C
Alignment length	154.0
HSP length	154.0
Score	793.0
Bit	310.07099999999997
e-value	3.0339099999997105e-115
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	3.0740399999999756e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	3.0740399999999756e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F, G, H, I, J, K, L
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A, B, C, D, E, F
Alignment length	154.0
HSP length	153.0
Score	786.0
Bit	307.375
e-value	2.9503999999999956e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	A
Alignment length	154.0
HSP length	153.0
Score	784.0
Bit	306.605
e-value	9.849589999999001e-114
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

Blastp Info
Chain	H
Alignment length	154.0
HSP length	152.0
Score	780.0
Bit	305.064
e-value	2.1040399999999876e-113
Similarity	1.0
Gaps	0.0

ClinVar Info
Accession	NA
Title	NA
Variant type	NA
Protein change	NA
Aliases	NA
Clinical significance	NA
Last evaluated	NA
Review status	NA
Associated traits	NA
dbs_and_accessions	NA

View builder

This tool allows you to create custom anchor elements that control the protein. See documentation for more.

Zoom to

residue domain clash surface bfactor auto default orientation

Selection

Color

Title

Radius

Tolerance

Show ligands

Orientation

Freeze

The orientation of the protein differs from the stored one above.

Add additional residue selections

<span class="prolink" data-toggle="viewport">Change a setting!</span>

Selection

Option A. Selection language

For more information on the NGL selection language see NGL manual

This controls the residues to focus on. The selection uses the NGL selection language. 1:A will select residue 1 of chain A, 1-20:B the residues 1 to 20 of chain B, * for everything, PLP (or [PLP]123:D) will select the residue named PLP (a ligand).
The logical operators and and or can also be used, e.g. :B or :C will select chains B & C. You can only select residues that exist in the structure, if not it will either show all or erroneously pan off camera when manually written. In this builder you will not be allowed to.
Also to prevent memory issues in mobiles the limit, in the builder only, for residue mode is 500 atoms.

To select two different elements use the logical operator or, not and, because you want to select anything that matches X or Y.

Selection line

Option B. Build Selection

The following is simpler, but much more limited that the previous.

Select a residue

Select a residue range

–

What to show residue and not the domain, or vice-versa? For the full list close this, and select the appropriate focusing mode (labelled "zoom to").

MUTAFY

Mutafy result for your input 6d2d346d33bc454595719f83d2bbaf85

Length

Best Mutant and Wildtype Protein Structures for your Input Genes

Configure initial view

Residue numbering mismatch

Predicted model

Engineered residues

Additional Infomation

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Mutafy result for your input
6d2d346d33bc454595719f83d2bbaf85