6ONS
Crystal structure of Desulfovibrio vulgaris carbon monoxide dehydrogenase with the D-cluster ligating cysteines mutated to alanines, coexpressed with CooC, as-isolated
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
| A | 0050418 | molecular_function | hydroxylamine reductase activity |
| 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 | 8 |
| Details | binding site for residue SF4 A 701 |
| Chain | Residue |
| A | CYS51 |
| A | CYS54 |
| A | MET56 |
| A | CYS59 |
| A | VAL73 |
| A | CYS74 |
| A | ARG84 |
| A | MET203 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue XCC A 702 |
| Chain | Residue |
| A | CYS301 |
| A | CYS302 |
| A | CYS340 |
| A | GLY447 |
| A | CYS448 |
| A | CYS478 |
| A | CYS519 |
| A | TYR553 |
| A | SER554 |
| A | LYS556 |
| A | HOH814 |
| A | HIS266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30277213","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31296570","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6B6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6DC2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ONC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OND","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PIRSR","id":"PIRSR005023-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30277213","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31296570","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35278753","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6B6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6DC2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ONC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OND","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ONS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TSJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PIRSR","id":"PIRSR005023-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30277213","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32655979","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6B6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6B6X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6DC2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6VWY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Binds C cluster in the oxidized state, but not in the canonical reduced state","evidences":[{"source":"PubMed","id":"30277213","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
