3L9Y
Crystal structures of holo and Cu-deficient Cu/ZnSOD from the silkworm Bombyx mori and the implications in Amyotrophic lateral sclerosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006801 | biological_process | superoxide metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006801 | biological_process | superoxide metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 155 |
| Chain | Residue |
| B | HIS62 |
| B | HIS70 |
| B | HIS79 |
| B | ASP82 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 155 |
| Chain | Residue |
| A | HIS62 |
| A | HIS70 |
| A | HIS79 |
| A | ASP82 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 156 |
| Chain | Residue |
| B | HIS47 |
| B | HIS62 |
| B | HIS120 |
| B | HIS45 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 156 |
| Chain | Residue |
| A | HIS45 |
| A | HIS47 |
| A | HIS62 |
| A | HIS120 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20310068, ECO:0007744|PDB:3L9Y |
| Chain | Residue | Details |
| A | HIS45 | |
| A | HIS47 | |
| A | HIS120 | |
| B | HIS45 | |
| B | HIS47 | |
| B | HIS120 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20310068, ECO:0007744|PDB:3L9E, ECO:0007744|PDB:3L9Y |
| Chain | Residue | Details |
| A | HIS62 | |
| A | HIS70 | |
| A | HIS79 | |
| A | ASP82 | |
| B | HIS62 | |
| B | HIS70 | |
| B | HIS79 | |
| B | ASP82 |
