7NP8
Crystal structure of the Coenzyme F420-dependent sulfite reductase from Methanocaldococcus jannaschii at 2.3-A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0052592 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0052592 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0052592 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0052592 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CaRCGtCTiVCP |
| Chain | Residue | Details |
| A | CYS15-PRO26 | |
| A | CYS524-PRO535 |
| site_id | PS00365 |
| Number of Residues | 17 |
| Details | NIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. SGCpngCvrpqvhDIGI |
| Chain | Residue | Details |
| A | SER466-ILE482 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00711 |
| Chain | Residue | Details |
| A | CYS15 | |
| A | CYS527 | |
| A | CYS530 | |
| A | CYS534 | |
| B | CYS15 | |
| B | CYS18 | |
| B | CYS21 | |
| B | CYS25 | |
| B | CYS495 | |
| B | CYS498 | |
| B | CYS501 | |
| A | CYS18 | |
| B | CYS505 | |
| B | CYS524 | |
| B | CYS527 | |
| B | CYS530 | |
| B | CYS534 | |
| C | CYS15 | |
| C | CYS18 | |
| C | CYS21 | |
| C | CYS25 | |
| C | CYS495 | |
| A | CYS21 | |
| C | CYS498 | |
| C | CYS501 | |
| C | CYS505 | |
| C | CYS524 | |
| C | CYS527 | |
| C | CYS530 | |
| C | CYS534 | |
| D | CYS15 | |
| D | CYS18 | |
| D | CYS21 | |
| A | CYS25 | |
| D | CYS25 | |
| D | CYS495 | |
| D | CYS498 | |
| D | CYS501 | |
| D | CYS505 | |
| D | CYS524 | |
| D | CYS527 | |
| D | CYS530 | |
| D | CYS534 | |
| A | CYS495 | |
| A | CYS498 | |
| A | CYS501 | |
| A | CYS505 | |
| A | CYS524 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q59109 |
| Chain | Residue | Details |
| A | CYS428 | |
| D | CYS428 | |
| D | CYS434 | |
| D | CYS468 | |
| A | CYS434 | |
| A | CYS468 | |
| B | CYS428 | |
| B | CYS434 | |
| B | CYS468 | |
| C | CYS428 | |
| C | CYS434 | |
| C | CYS468 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:Q59109 |
| Chain | Residue | Details |
| A | CYS472 | |
| B | CYS472 | |
| C | CYS472 | |
| D | CYS472 |
