Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008398 | molecular_function | sterol 14-demethylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0032541 | cellular_component | cortical endoplasmic reticulum |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097038 | cellular_component | perinuclear endoplasmic reticulum |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue HEM A 601 |
| Chain | Residue |
| A | PHE114 |
| A | PRO380 |
| A | LEU384 |
| A | ARG386 |
| A | PRO464 |
| A | PHE465 |
| A | GLY466 |
| A | HIS470 |
| A | CYS472 |
| A | ILE473 |
| A | GLY474 |
| A | TYR127 |
| A | PHE477 |
| A | ALA478 |
| A | 1YN602 |
| A | HOH732 |
| A | TYR141 |
| A | LEU148 |
| A | LYS152 |
| A | VAL312 |
| A | GLY315 |
| A | GLY316 |
| A | THR319 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue 1YN A 602 |
| Chain | Residue |
| A | ALA70 |
| A | TYR73 |
| A | TYR127 |
| A | ILE140 |
| A | PHE237 |
| A | GLY311 |
| A | VAL312 |
| A | GLY315 |
| A | THR319 |
| A | HIS382 |
| A | SER383 |
| A | PHE385 |
| A | PHE509 |
| A | THR510 |
| A | SER511 |
| A | MET512 |
| A | HEM601 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 603 |
| Chain | Residue |
| A | PRO422 |
| A | GLU426 |
| A | ASN428 |
| A | HIS430 |
| A | ARG431 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE A 604 |
| Chain | Residue |
| A | GLU217 |
| A | LYS221 |
| A | THR265 |
| A | SER268 |
| A | GLU272 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 605 |
| Chain | Residue |
| A | ARG180 |
| A | ASN188 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 606 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGRHRCIG |
| Chain | Residue | Details |
| A | PHE465-GLY474 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
