4YT3
CYP106A2
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 | 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 |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | ILE88 |
| A | LEU294 |
| A | ARG296 |
| A | THR347 |
| A | PHE348 |
| A | HIS353 |
| A | CYS355 |
| A | GLY357 |
| A | HOH661 |
| A | HOH665 |
| A | HOH715 |
| A | THR89 |
| A | HOH822 |
| A | HIS96 |
| A | ARG100 |
| A | MET151 |
| A | ALA243 |
| A | GLY244 |
| A | THR247 |
| A | THR248 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 502 |
| Chain | Residue |
| A | PRO93 |
| A | HIS96 |
| A | ARG97 |
| A | PRO352 |
| A | HOH604 |
| A | HOH869 |
| B | VAL35 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | ILE88 |
| B | THR89 |
| B | HIS96 |
| B | ARG100 |
| B | ALA243 |
| B | GLY244 |
| B | THR247 |
| B | THR248 |
| B | LEU294 |
| B | ARG296 |
| B | MET319 |
| B | THR347 |
| B | PHE348 |
| B | PRO352 |
| B | HIS353 |
| B | CYS355 |
| B | GLY357 |
| B | HOH664 |
| B | HOH672 |
| B | HOH693 |
| B | HOH808 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 502 |
| Chain | Residue |
| A | VAL35 |
| B | PRO93 |
| B | HIS96 |
| B | ARG97 |
| B | HOH752 |
| B | HOH753 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGPHFCLG |
| Chain | Residue | Details |
| A | PHE348-GLY357 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS355 | |
| B | CYS355 |
