1OA1
REDUCED HYBRID CLUSTER PROTEIN (HCP) FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH STRUCTURE AT 1.55A RESOLUTION USING SYNCHROTRON RADIATION.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050418 | molecular_function | hydroxylamine reductase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1554 |
| Chain | Residue |
| A | CYS3 |
| A | LYS23 |
| A | THR71 |
| A | PHE4 |
| A | GLN5 |
| A | CYS6 |
| A | THR9 |
| A | CYS15 |
| A | GLY19 |
| A | MET20 |
| A | CYS21 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF3 A 1555 |
| Chain | Residue |
| A | HIS244 |
| A | GLU268 |
| A | TRP292 |
| A | CYS312 |
| A | CYS406 |
| A | CYS434 |
| A | CYS459 |
| A | GLU494 |
| A | HOH2767 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1556 |
| Chain | Residue |
| A | ASN273 |
| A | LYS279 |
| A | TYR281 |
| A | PHE284 |
| A | VAL285 |
| A | HOH2817 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1557 |
| Chain | Residue |
| A | GLY14 |
| A | CYS15 |
| A | THR16 |
| A | VAL17 |
| A | LYS18 |
| A | HOH2818 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | CYS3 | |
| A | CYS6 | |
| A | CYS15 | |
| A | CYS21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12 |
| Chain | Residue | Details |
| A | HIS244 | |
| A | GLU268 | |
| A | CYS312 | |
| A | CYS434 | |
| A | CYS459 | |
| A | GLU494 | |
| A | LYS496 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: via persulfide group => ECO:0000269|PubMed:11106482, ECO:0000269|PubMed:11941509, ECO:0000269|PubMed:12764602, ECO:0000269|PubMed:18560155, ECO:0000269|Ref.12 |
| Chain | Residue | Details |
| A | CYS406 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Cysteine persulfide => ECO:0000269|PubMed:11941509 |
| Chain | Residue | Details |
| A | CYS406 |
