6B6Y
Crystal structure of Desulfovibrio vulgaris carbon monoxide dehydrogenase, dithionite-reduced then oxygen-exposed (protein batch 2), oxidized C-cluster
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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0016151 | molecular_function | nickel cation binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
| B | 0050418 | molecular_function | hydroxylamine reductase activity |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 A 701 |
| Chain | Residue |
| A | CYS51 |
| A | CYS54 |
| A | MET56 |
| A | CYS59 |
| A | CYS74 |
| A | ARG84 |
| A | MET203 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue CUV A 702 |
| Chain | Residue |
| A | CYS302 |
| A | CYS340 |
| A | GLY447 |
| A | CYS448 |
| A | GLY477 |
| A | CYS478 |
| A | CYS519 |
| A | TYR553 |
| A | SER554 |
| A | LYS556 |
| A | HIS266 |
| A | CYS301 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 703 |
| Chain | Residue |
| A | GLU421 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue FES B 701 |
| Chain | Residue |
| A | CYS42 |
| A | CYS45 |
| A | THR50 |
| B | CYS42 |
| B | CYS45 |
| B | THR50 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 702 |
| Chain | Residue |
| B | CYS51 |
| B | CYS54 |
| B | MET56 |
| B | CYS59 |
| B | CYS74 |
| B | ARG84 |
| B | MET203 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue CUV B 703 |
| Chain | Residue |
| B | HIS266 |
| B | CYS301 |
| B | CYS302 |
| B | CYS340 |
| B | GLY447 |
| B | CYS448 |
| B | GLY477 |
| B | CYS478 |
| B | CYS519 |
| B | TYR553 |
| B | SER554 |
| B | LYS556 |
