5Z9J
Identification of the functions of unusual cytochrome p450-like monooxygenases involved in microbial secondary metablism
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM A 401 |
| Chain | Residue |
| A | PHE75 |
| A | ARG289 |
| A | GLY339 |
| A | LEU340 |
| A | GLY341 |
| A | ILE344 |
| A | HIS345 |
| A | CYS347 |
| A | GLY349 |
| A | HOH551 |
| A | HOH558 |
| A | ALA76 |
| A | HOH591 |
| A | HIS83 |
| A | ARG87 |
| A | ASN237 |
| A | GLY238 |
| A | THR241 |
| A | THR242 |
| A | LEU245 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue TAM A 402 |
| Chain | Residue |
| A | GLY14 |
| A | TRP17 |
| A | ASN37 |
| A | TYR39 |
| A | TRP311 |
| A | VAL385 |
| A | HOH516 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue HEM B 401 |
| Chain | Residue |
| B | PHE75 |
| B | ALA76 |
| B | HIS83 |
| B | ARG87 |
| B | LEU234 |
| B | ASN237 |
| B | GLY238 |
| B | THR241 |
| B | LEU245 |
| B | ARG289 |
| B | GLY339 |
| B | LEU340 |
| B | GLY341 |
| B | HIS345 |
| B | CYS347 |
| B | GLY349 |
| B | HOH526 |
| B | HOH535 |
| B | HOH549 |
| B | HOH558 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue HEM C 401 |
| Chain | Residue |
| C | PHE75 |
| C | ALA76 |
| C | HIS83 |
| C | ARG87 |
| C | LEU234 |
| C | ASN237 |
| C | GLY238 |
| C | THR241 |
| C | THR242 |
| C | LEU245 |
| C | ARG289 |
| C | GLY339 |
| C | LEU340 |
| C | GLY341 |
| C | ILE344 |
| C | HIS345 |
| C | CYS347 |
| C | LEU348 |
| C | GLY349 |
| C | ALA353 |
| C | HOH534 |
| C | HOH542 |
| C | HOH556 |
| C | HOH564 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue TAM C 402 |
| Chain | Residue |
| C | GLY14 |
| C | ASP30 |
| C | ASN37 |
| C | TYR39 |
| C | TRP311 |
| C | VAL385 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue HEM D 401 |
| Chain | Residue |
| D | PHE75 |
| D | ALA76 |
| D | HIS83 |
| D | ARG87 |
| D | LEU234 |
| D | ASN237 |
| D | GLY238 |
| D | THR241 |
| D | THR242 |
| D | ILE284 |
| D | ARG289 |
| D | GLY339 |
| D | LEU340 |
| D | GLY341 |
| D | HIS345 |
| D | CYS347 |
| D | GLY349 |
| D | ALA353 |
| D | HOH524 |
| D | HOH532 |
| D | HOH560 |
| D | HOH596 |
