8RQZ
Crystal structure of Molybdenum bispyranopterin guanine dinucleotide formate dehydrogenases ForCE1 from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0009326 | cellular_component | formate dehydrogenase complex |
| A | 0015944 | biological_process | formate oxidation |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0009326 | cellular_component | formate dehydrogenase complex |
| B | 0015944 | biological_process | formate oxidation |
| C | 0003954 | molecular_function | NADH dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| C | 0009326 | cellular_component | formate dehydrogenase complex |
| C | 0015942 | biological_process | formate metabolic process |
| C | 0015944 | biological_process | formate oxidation |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0036397 | molecular_function | formate dehydrogenase (quinone) activity |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0003954 | molecular_function | NADH dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| D | 0009326 | cellular_component | formate dehydrogenase complex |
| D | 0015942 | biological_process | formate metabolic process |
| D | 0015944 | biological_process | formate oxidation |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0036397 | molecular_function | formate dehydrogenase (quinone) activity |
| D | 0043546 | molecular_function | molybdopterin cofactor binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Domain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 62 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 58 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 112 |
| Details | Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"40855134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8RQZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9GZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"40855134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8RQZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9GZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"40855134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"40855134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8RQZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9GZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"40855134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8RQZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"40855134","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8RQZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RR0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9GZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
