Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | TYR66 |
| A | GLY247 |
| A | GLY248 |
| A | THR251 |
| A | SER252 |
| A | SER255 |
| A | PRO293 |
| A | PHE297 |
| A | ARG299 |
| A | THR349 |
| A | PHE350 |
| A | ASN78 |
| A | GLY351 |
| A | HIS355 |
| A | CYS357 |
| A | GLY359 |
| A | PGE516 |
| A | HOH629 |
| A | HOH630 |
| A | LEU95 |
| A | ALA96 |
| A | HIS103 |
| A | ARG107 |
| A | LEU161 |
| A | SER243 |
| A | LEU244 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | HIS-3 |
| A | PHE263 |
| A | PRO267 |
| A | TRP270 |
| A | GLY380 |
| A | PHE381 |
| A | HOH696 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ALA333 |
| A | ASP339 |
| A | ARG342 |
| A | HOH987 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | GLU329 |
| A | ALA333 |
| A | HOH851 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | PRO121 |
| A | GLN125 |
| A | ASP160 |
| A | HOH741 |
| A | HOH998 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | THR2 |
| A | ILE383 |
| A | THR384 |
| A | GLY385 |
| A | HOH907 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | PRO9 |
| A | ASP10 |
| A | ASP11 |
| A | THR14 |
| A | HOH788 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | SER13 |
| A | ILE15 |
| A | ASN16 |
| A | PRO45 |
| A | HOH1003 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 511 |
| Chain | Residue |
| A | ARG21 |
| A | VAL25 |
| A | HOH859 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 512 |
| Chain | Residue |
| A | GLU250 |
| A | HOH875 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 513 |
| Chain | Residue |
| A | THR215 |
| A | ASP217 |
| A | HOH962 |
| A | HOH998 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 514 |
| Chain | Residue |
| A | THR73 |
| A | LYS76 |
| A | ALA301 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 515 |
| Chain | Residue |
| A | THR303 |
| A | ASP304 |
| A | ALA314 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PGE A 516 |
| Chain | Residue |
| A | ASN78 |
| A | ALA96 |
| A | SER243 |
| A | GLY247 |
| A | THR251 |
| A | PHE297 |
| A | HEM501 |
| A | HOH805 |
| A | HOH922 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGPHFCLG |
| Chain | Residue | Details |
| A | PHE350-GLY359 | |
