Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006082 | biological_process | organic acid metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008392 | molecular_function | arachidonate epoxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| A | 0019373 | biological_process | epoxygenase P450 pathway |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | PHE220 |
| A | ARG434 |
| A | CYS436 |
| A | TMI501 |
| A | CM5504 |
| A | HOH610 |
| A | HOH632 |
| A | HOH670 |
| A | THR302 |
| A | THR306 |
| A | VAL367 |
| A | HIS369 |
| A | LEU392 |
| A | PRO428 |
| A | PHE429 |
| A | SER430 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TMI A 501 |
| Chain | Residue |
| A | SER128 |
| A | MET132 |
| A | SER213 |
| A | PHE217 |
| A | PHE220 |
| A | LEU295 |
| A | PHE296 |
| A | ALA298 |
| A | GLY299 |
| A | THR302 |
| A | ILE363 |
| A | HEM500 |
| A | CM5504 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TMI A 502 |
| Chain | Residue |
| A | PRO106 |
| A | PHE184 |
| A | LEU198 |
| A | PHE202 |
| A | ASN287 |
| A | LEU290 |
| A | THR291 |
| A | LEU293 |
| A | SER294 |
| A | PHE297 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TMI A 503 |
| Chain | Residue |
| A | GLN45 |
| A | MET46 |
| A | ARG48 |
| A | LEU51 |
| A | VAL68 |
| A | TYR69 |
| A | LEU70 |
| A | VAL104 |
| A | GLU218 |
| A | PHE223 |
| A | PHE365 |
| A | VAL477 |
| A | CM5507 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CM5 A 504 |
| Chain | Residue |
| A | GLU93 |
| A | PHE108 |
| A | ARG125 |
| A | LEU129 |
| A | LEU219 |
| A | LYS433 |
| A | HEM500 |
| A | TMI501 |
| A | HOH610 |
| A | HOH663 |
| A | HOH678 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CM5 A 505 |
| Chain | Residue |
| A | ARG98 |
| A | ILE101 |
| A | ILE114 |
| A | PHE115 |
| A | GLY118 |
| A | ARG122 |
| A | TYR226 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CM5 A 506 |
| Chain | Residue |
| A | LEU40 |
| A | VAL249 |
| A | GLU250 |
| A | ARG253 |
| A | PHE264 |
| A | TYR268 |
| A | GLN286 |
| A | LEU293 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CM5 A 507 |
| Chain | Residue |
| A | PRO34 |
| A | SER35 |
| A | LEU37 |
| A | LEU51 |
| A | SER54 |
| A | ARG57 |
| A | PHE365 |
| A | TMI503 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSlGKRICLG |
| Chain | Residue | Details |
| A | PHE429-GLY438 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P00176","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR302 | |
| A | GLU301 | |
