1HL4
The Structure of Apo Type Human Cu, Zn Superoxide Dismutase
External Resource: Annotation
- Domain Annotation: SCOP/SCOPe Classification
- Domain Annotation: SCOP2 Classification
- Domain Annotation: ECOD Classification
- Domain Annotation: CATH
- Protein Family Annotation
- Gene Ontology: Gene Product Annotation
- InterPro: Protein Family Classification
- Pharos: Disease Associations
- Protein Modification Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
C | d1hl4c_ | All beta proteins | Immunoglobulin-like beta-sandwich | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase, SOD | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
A | d1hl4a_ | All beta proteins | Immunoglobulin-like beta-sandwich | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase, SOD | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
B | d1hl4b_ | All beta proteins | Immunoglobulin-like beta-sandwich | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase, SOD | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
D | d1hl4d_ | All beta proteins | Immunoglobulin-like beta-sandwich | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase-like | Cu,Zn superoxide dismutase, SOD | HUMAN (Homo sapiens ) [TaxId: 9606 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
C | SCOP2B Superfamily | Cu, Zn superoxide dismutase-like | 8055253 | 3002059 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Cu, Zn superoxide dismutase-like | 8055253 | 3002059 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Cu, Zn superoxide dismutase-like | 8055253 | 3002059 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Cu, Zn superoxide dismutase-like | 8055253 | 3002059 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
C | Sod_Cu | e1hl4C1 | A: beta sandwiches | X: Immunoglobulin-like beta-sandwich | H: Immunoglobulin-related | T: Cu,Zn superoxide dismutase-like | F: Sod_Cu | ECOD (1.6) |
A | Sod_Cu | e1hl4A1 | A: beta sandwiches | X: Immunoglobulin-like beta-sandwich | H: Immunoglobulin-related | T: Cu,Zn superoxide dismutase-like | F: Sod_Cu | ECOD (1.6) |
B | Sod_Cu | e1hl4B1 | A: beta sandwiches | X: Immunoglobulin-like beta-sandwich | H: Immunoglobulin-related | T: Cu,Zn superoxide dismutase-like | F: Sod_Cu | ECOD (1.6) |
D | Sod_Cu | e1hl4D1 | A: beta sandwiches | X: Immunoglobulin-like beta-sandwich | H: Immunoglobulin-related | T: Cu,Zn superoxide dismutase-like | F: Sod_Cu | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
C | 2.60.40.200 | Mainly Beta | Sandwich | Immunoglobulin-like | Superoxide dismutase, copper/zinc binding domain | CATH (4.3.0) |
A | 2.60.40.200 | Mainly Beta | Sandwich | Immunoglobulin-like | Superoxide dismutase, copper/zinc binding domain | CATH (4.3.0) |
B | 2.60.40.200 | Mainly Beta | Sandwich | Immunoglobulin-like | Superoxide dismutase, copper/zinc binding domain | CATH (4.3.0) |
D | 2.60.40.200 | Mainly Beta | Sandwich | Immunoglobulin-like | Superoxide dismutase, copper/zinc binding domain | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00080 | Copper/zinc superoxide dismutase (SODC) (Sod_Cu) | Copper/zinc superoxide dismutase (SODC) | superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SO ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR024134 | Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone | Family | |
IPR036423 | Superoxide dismutase-like, copper/zinc binding domain superfamily | Homologous Superfamily | |
IPR018152 | Superoxide dismutase, copper/zinc, binding site | Binding Site | |
IPR001424 | Superoxide dismutase, copper/zinc binding domain | Domain |
Pharos: Disease Associations Pharos Homepage Annotation
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
ACE | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 | :