3TYW
Crystal Structure of CYP105N1 from Streptomyces coelicolor A3(2)
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 | 0042440 | biological_process | pigment metabolic process |
| 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 | 0042440 | biological_process | pigment metabolic process |
| 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 | 0042440 | biological_process | pigment metabolic process |
| 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 | 0042440 | biological_process | pigment metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | ILE100 |
| A | ILE299 |
| A | PRO300 |
| A | ARG302 |
| A | ALA352 |
| A | HIS358 |
| A | CYS360 |
| A | GLY362 |
| A | HIS107 |
| A | ARG111 |
| A | PHE118 |
| A | THR246 |
| A | GLY250 |
| A | THR253 |
| A | THR254 |
| A | MET257 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | ILE100 |
| B | HIS107 |
| B | ARG111 |
| B | PHE118 |
| B | THR246 |
| B | GLY250 |
| B | THR253 |
| B | THR254 |
| B | MET257 |
| B | ILE299 |
| B | PRO300 |
| B | ARG302 |
| B | ALA352 |
| B | PHE353 |
| B | HIS358 |
| B | CYS360 |
| B | VAL361 |
| B | GLY362 |
| B | HOH606 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | ILE100 |
| C | HIS107 |
| C | ARG111 |
| C | PHE118 |
| C | THR246 |
| C | GLY250 |
| C | THR253 |
| C | THR254 |
| C | MET257 |
| C | ALA296 |
| C | PRO300 |
| C | ARG302 |
| C | LEU325 |
| C | ALA352 |
| C | HIS358 |
| C | CYS360 |
| C | VAL361 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | ILE100 |
| D | HIS107 |
| D | ARG111 |
| D | PHE118 |
| D | THR246 |
| D | GLY250 |
| D | THR253 |
| D | THR254 |
| D | MET257 |
| D | PRO300 |
| D | ARG302 |
| D | LEU325 |
| D | ALA352 |
| D | HIS358 |
| D | CYS360 |
| D | VAL361 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGyGVHQCVG |
| Chain | Residue | Details |
| A | PHE353-GLY362 |
