3NC6
CYP134A1 1-phenylimidazole bound structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016713 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046148 | biological_process | pigment biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0016713 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046148 | biological_process | pigment biosynthetic process |
| 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 406 |
| Chain | Residue |
| A | SER63 |
| A | VAL280 |
| A | ILE283 |
| A | ARG285 |
| A | ALA345 |
| A | PHE346 |
| A | HIS351 |
| A | CYS353 |
| A | VAL354 |
| A | GLY355 |
| A | PHE358 |
| A | LEU64 |
| A | PIW407 |
| A | ILE97 |
| A | MET143 |
| A | ASN229 |
| A | ALA233 |
| A | ALA234 |
| A | PRO237 |
| A | THR241 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 406 |
| Chain | Residue |
| B | SER63 |
| B | LEU64 |
| B | ILE97 |
| B | ASN229 |
| B | ALA233 |
| B | ALA234 |
| B | PRO237 |
| B | THR241 |
| B | ILE283 |
| B | ARG285 |
| B | ALA345 |
| B | PHE346 |
| B | HIS351 |
| B | CYS353 |
| B | GLY355 |
| B | PHE358 |
| B | GLU362 |
| B | PIW407 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PIW A 407 |
| Chain | Residue |
| A | LEU64 |
| A | LEU232 |
| A | GLU236 |
| A | HEM406 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PIW B 407 |
| Chain | Residue |
| B | LEU64 |
| B | GLU236 |
| B | THR392 |
| B | HEM406 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGIHNCVG |
| Chain | Residue | Details |
| A | PHE346-GLY355 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20690619 |
| Chain | Residue | Details |
| A | LYS62 | |
| A | ASN229 | |
| A | ARG285 | |
| B | LYS62 | |
| B | ASN229 | |
| B | ARG285 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS353 | |
| B | CYS353 |
