Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | HIS75 |
| A | THR253 |
| A | MET256 |
| A | ARG303 |
| A | ALA355 |
| A | PHE356 |
| A | GLY357 |
| A | HIS361 |
| A | CYS363 |
| A | GLY365 |
| A | ALA369 |
| A | PHE99 |
| A | HOH652 |
| A | HOH654 |
| A | HOH682 |
| A | HOH725 |
| A | ALA100 |
| A | HIS107 |
| A | ARG111 |
| A | PHE118 |
| A | ALA248 |
| A | GLY249 |
| A | THR252 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 502 |
| Chain | Residue |
| A | ALA100 |
| A | THR300 |
| A | HOH634 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | HIS75 |
| B | PHE99 |
| B | ALA100 |
| B | HIS107 |
| B | ARG111 |
| B | PHE118 |
| B | MET244 |
| B | LEU245 |
| B | ALA248 |
| B | GLY249 |
| B | THR252 |
| B | THR253 |
| B | MET256 |
| B | VAL301 |
| B | ARG303 |
| B | ALA355 |
| B | PHE356 |
| B | VAL360 |
| B | HIS361 |
| B | CYS363 |
| B | ALA369 |
| B | HOH638 |
| B | HOH658 |
| B | HOH662 |
| B | HOH704 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 502 |
| Chain | Residue |
| B | THR252 |
| B | THR300 |
| B | HOH638 |
| B | HOH735 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 503 |
| Chain | Residue |
| B | ALA202 |
| B | ASP236 |
| B | HOH724 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGVHQCLG |
| Chain | Residue | Details |
| A | PHE356-GLY365 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28869713","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y1I","evidenceCode":"ECO:0007744"}]} |
