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 | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0008392 | molecular_function | arachidonic acid epoxygenase activity |
A | 0016020 | cellular_component | membrane |
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 | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0046872 | molecular_function | metal ion binding |
A | 0070330 | molecular_function | aromatase activity |
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: axial binding residue |
Chain | Residue | Details |
A | ASN456 | |
Chain | Residue | Details |
A | GLU148 | |
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 | |