3VEE
Rhodococcus jostii RHA1 DypB N246A variant in complex with heme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | ASP147 |
| A | HIS189 |
| A | ARG208 |
| A | HIS226 |
| A | VAL227 |
| A | ASN230 |
| A | ARG244 |
| A | PHE261 |
| A | THR271 |
| A | MET274 |
| A | MET278 |
| A | PHE151 |
| A | SER294 |
| A | HOH528 |
| A | HOH531 |
| A | HOH533 |
| A | HOH551 |
| A | HOH655 |
| A | VAL152 |
| A | ASP153 |
| A | GLY154 |
| A | THR155 |
| A | GLU156 |
| A | GLN185 |
| A | TYR187 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 402 |
| Chain | Residue |
| A | LYS113 |
| A | PHE117 |
| A | HIS138 |
| A | HOH509 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 401 |
| Chain | Residue |
| B | ASP147 |
| B | PHE151 |
| B | VAL152 |
| B | ASP153 |
| B | GLY154 |
| B | THR155 |
| B | GLU156 |
| B | GLN185 |
| B | TYR187 |
| B | HIS189 |
| B | ARG208 |
| B | HIS226 |
| B | ASN230 |
| B | ARG244 |
| B | PHE261 |
| B | MET274 |
| B | MET278 |
| B | SER294 |
| B | HOH572 |
| B | HOH573 |
| B | HOH582 |
| B | HOH644 |
| B | HOH645 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 402 |
| Chain | Residue |
| B | LYS113 |
| B | PHE117 |
| B | HIS138 |
| B | HOH538 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 403 |
| Chain | Residue |
| B | ALA82 |
| B | HIS83 |
| B | HIS85 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM C 401 |
| Chain | Residue |
| C | ASP147 |
| C | PHE151 |
| C | VAL152 |
| C | ASP153 |
| C | GLY154 |
| C | THR155 |
| C | GLU156 |
| C | GLN185 |
| C | TYR187 |
| C | HIS189 |
| C | ARG208 |
| C | HIS226 |
| C | VAL227 |
| C | ASN230 |
| C | ARG244 |
| C | THR259 |
| C | PHE261 |
| C | MET274 |
| C | LEU275 |
| C | MET278 |
| C | SER294 |
| C | HOH537 |
| C | HOH556 |
| C | HOH583 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 402 |
| Chain | Residue |
| C | LYS113 |
| C | PHE117 |
| C | HIS138 |
| C | HOH547 |
