3OFU
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 |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| F | 0020037 | molecular_function | heme binding |
| F | 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 417 |
| Chain | Residue |
| A | TRP61 |
| A | VAL239 |
| A | VAL283 |
| A | ARG285 |
| A | THR337 |
| A | MET338 |
| A | GLY339 |
| A | HIS343 |
| A | CYS345 |
| A | VAL346 |
| A | LEU350 |
| A | PRO86 |
| A | ALA351 |
| A | LEU87 |
| A | HIS94 |
| A | ARG98 |
| A | ASN230 |
| A | LEU231 |
| A | GLY234 |
| A | THR238 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ID3 A 397 |
| Chain | Residue |
| A | LEU78 |
| A | VAL384 |
| 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 | VAL239 |
| B | MET242 |
| B | VAL281 |
| B | VAL283 |
| B | ARG285 |
| B | THR337 |
| B | MET338 |
| B | GLY339 |
| B | ALA342 |
| B | HIS343 |
| B | CYS345 |
| B | VAL346 |
| B | ALA351 |
| B | GLU354 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ID3 B 397 |
| Chain | Residue |
| B | LEU78 |
| B | ASN383 |
| B | VAL384 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 417 |
| Chain | Residue |
| C | TRP61 |
| C | PRO86 |
| C | LEU87 |
| C | HIS94 |
| C | ARG98 |
| C | LEU105 |
| C | ASN230 |
| C | LEU231 |
| C | GLY234 |
| C | GLY235 |
| C | THR238 |
| C | VAL239 |
| C | VAL283 |
| C | ARG285 |
| C | THR337 |
| C | MET338 |
| C | GLY339 |
| C | HIS343 |
| C | CYS345 |
| C | VAL346 |
| C | ALA351 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ID3 C 397 |
| Chain | Residue |
| C | GLY234 |
| C | ASN383 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM D 417 |
| Chain | Residue |
| D | TRP61 |
| D | PRO86 |
| D | LEU87 |
| D | HIS94 |
| D | ARG98 |
| D | ASN230 |
| D | LEU231 |
| D | GLY234 |
| D | GLY235 |
| D | THR238 |
| D | VAL239 |
| D | VAL283 |
| D | ARG285 |
| D | THR337 |
| D | MET338 |
| D | GLY339 |
| D | ALA342 |
| D | HIS343 |
| D | CYS345 |
| D | VAL346 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM E 417 |
| Chain | Residue |
| E | GLY234 |
| E | THR238 |
| E | MET242 |
| E | VAL283 |
| E | ARG285 |
| E | THR337 |
| E | MET338 |
| E | GLY339 |
| E | HIS343 |
| E | CYS345 |
| E | VAL346 |
| E | TRP61 |
| E | PRO86 |
| E | LEU87 |
| E | HIS94 |
| E | ARG98 |
| E | ASN230 |
| E | LEU231 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM F 417 |
| Chain | Residue |
| F | TRP61 |
| F | PRO86 |
| F | LEU87 |
| F | HIS94 |
| F | ARG98 |
| F | ASN230 |
| F | LEU231 |
| F | GLY234 |
| F | THR238 |
| F | VAL239 |
| F | MET242 |
| F | VAL283 |
| F | ARG285 |
| F | THR337 |
| F | MET338 |
| F | GLY339 |
| F | HIS343 |
| F | CYS345 |
| F | VAL346 |
| F | ALA351 |
| F | GLU354 |
