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 | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0009975 | molecular_function | cyclase 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 | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| 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 |
| A | 0070025 | molecular_function | carbon monoxide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ARG58 |
| A | SER61 |
| A | MET62 |
| A | LYS63 |
| A | HIS343 |
| A | HOH792 |
| A | HOH831 |
| A | HOH1076 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ARG17 |
| A | HOH673 |
| A | HOH713 |
| A | HOH768 |
| A | HOH886 |
| A | SER12 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | VAL5 |
| A | LEU6 |
| A | LEU7 |
| A | ARG32 |
| A | ARG300 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | ARG134 |
| A | PHE161 |
| A | ARG381 |
| A | ARG391 |
| A | HOH563 |
| A | HOH576 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 405 |
| Chain | Residue |
| A | MET62 |
| A | MET86 |
| A | HIS146 |
| A | PHE230 |
| A | GLY234 |
| A | SER237 |
| A | PHE280 |
| A | LEU284 |
| A | ARG286 |
| A | ALA337 |
| A | PHE338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | PRO346 |
| A | 1ED406 |
| A | HOH501 |
| A | HOH524 |
| A | HOH567 |
| A | HOH614 |
| A | HOH724 |
| A | HOH1057 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1ED A 406 |
| Chain | Residue |
| A | VAL78 |
| A | VAL82 |
| A | VAL83 |
| A | ASN85 |
| A | ALA167 |
| A | PHE168 |
| A | THR229 |
| A | HEM405 |
| A | HOH540 |
| A | HOH567 |
| A | HOH624 |
| A | HOH753 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG |
| Chain | Residue | Details |
| A | PHE338-GLY347 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | THR77 | |
| A | SER237 | |
| A | LYS301 | |
| A | GLN385 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN85 | |
| Chain | Residue | Details |
| A | ARG286 | |
| A | HIS343 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS345 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Participates in a stacking interactions with the tyrosyl of cYY |
| Chain | Residue | Details |
| A | PHE168 | |
| A | TRP182 | |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Important for the position of heme |
| Chain | Residue | Details |
| A | PRO346 | |
