3OFT
Crystal Structure of Cytochrome P450 CYP101C1
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 | 0020037 | molecular_function | heme binding |
| 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 | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 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 417 |
| Chain | Residue |
| A | TRP61 |
| A | THR238 |
| A | MET242 |
| A | VAL283 |
| A | ARG285 |
| A | THR337 |
| A | MET338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | VAL346 |
| A | PRO86 |
| A | ALA351 |
| A | GLU354 |
| A | HX2397 |
| A | HOH398 |
| A | HOH461 |
| A | HOH469 |
| A | HOH526 |
| A | LEU87 |
| A | HIS94 |
| A | ARG98 |
| A | ASN230 |
| A | LEU231 |
| A | GLY234 |
| A | GLY235 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HX2 A 397 |
| Chain | Residue |
| A | ALA282 |
| A | ASN383 |
| A | HOH398 |
| A | HEM417 |
| A | HOH521 |
| A | HOH618 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM B 417 |
| Chain | Residue |
| B | TRP61 |
| B | PRO86 |
| B | LEU87 |
| B | HIS94 |
| B | ARG98 |
| B | ASN230 |
| B | LEU231 |
| B | GLY234 |
| B | GLY235 |
| B | THR238 |
| B | MET242 |
| B | VAL283 |
| B | ARG285 |
| B | THR337 |
| B | MET338 |
| B | GLY339 |
| B | HIS343 |
| B | CYS345 |
| B | VAL346 |
| B | ALA351 |
| B | HOH399 |
| B | HOH459 |
| B | HOH518 |
| B | HOH604 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HX2 B 397 |
| Chain | Residue |
| B | ALA282 |
| B | VAL283 |
| B | ASN383 |
| B | HOH399 |
| B | HOH487 |
| B | HOH518 |
| B | HOH519 |
| B | HOH600 |
| B | HOH612 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM C 417 |
| Chain | Residue |
| C | TRP61 |
| C | PRO86 |
| C | LEU87 |
| C | HIS94 |
| C | ARG98 |
| C | ASN230 |
| C | LEU231 |
| C | GLY234 |
| C | GLY235 |
| C | THR238 |
| C | MET242 |
| C | VAL283 |
| C | ARG285 |
| C | THR337 |
| C | MET338 |
| C | GLY339 |
| C | HIS343 |
| C | CYS345 |
| C | VAL346 |
| C | HX2397 |
| C | HOH398 |
| C | HOH410 |
| C | HOH499 |
| C | HOH542 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HX2 C 397 |
| Chain | Residue |
| C | LEU72 |
| C | ALA282 |
| C | VAL283 |
| C | ASN383 |
| C | HOH398 |
| C | HEM417 |
| C | HOH437 |
| C | HOH441 |
| C | HOH475 |
