4G3J
Sterol 14-alpha demethylase (CYP51) from Trypanosoma brucei in complex with the VNI derivative (R)-N-(1-(2,4-dichlorophenyl)-2-(1H-1,2,4-triazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxadiazol-2-yl)benzamide [R-VNI-triazole (VNT)]
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005635 | cellular_component | nuclear envelope |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0008398 | molecular_function | sterol 14-demethylase activity |
| A | 0016125 | biological_process | sterol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase 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 | 0044091 | biological_process | membrane biogenesis |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005635 | cellular_component | nuclear envelope |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0008398 | molecular_function | sterol 14-demethylase activity |
| B | 0016125 | biological_process | sterol metabolic process |
| B | 0016491 | molecular_function | oxidoreductase 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 | 0044091 | biological_process | membrane biogenesis |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005635 | cellular_component | nuclear envelope |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0008398 | molecular_function | sterol 14-demethylase activity |
| C | 0016125 | biological_process | sterol metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0044091 | biological_process | membrane biogenesis |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005635 | cellular_component | nuclear envelope |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0008398 | molecular_function | sterol 14-demethylase activity |
| D | 0016125 | biological_process | sterol metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0044091 | biological_process | membrane biogenesis |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | TYR103 |
| A | ARG361 |
| A | GLY414 |
| A | PHE415 |
| A | GLY416 |
| A | HIS420 |
| A | LYS421 |
| A | CYS422 |
| A | ILE423 |
| A | GLY424 |
| A | VNT502 |
| A | TYR116 |
| A | HOH607 |
| A | HOH620 |
| A | HOH624 |
| A | ARG124 |
| A | ALA288 |
| A | ALA291 |
| A | GLY292 |
| A | THR295 |
| A | SER296 |
| A | LEU356 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VNT A 502 |
| Chain | Residue |
| A | PHE48 |
| A | TYR103 |
| A | PHE105 |
| A | PHE110 |
| A | TYR116 |
| A | PHE290 |
| A | ALA291 |
| A | THR295 |
| A | LEU356 |
| A | MET358 |
| A | MET360 |
| A | MET460 |
| A | HEM501 |
| A | HOH780 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | TYR116 |
| B | ARG124 |
| B | LEU134 |
| B | ALA288 |
| B | ALA291 |
| B | GLY292 |
| B | THR295 |
| B | SER296 |
| B | ARG361 |
| B | GLY414 |
| B | PHE415 |
| B | GLY416 |
| B | VAL419 |
| B | HIS420 |
| B | LYS421 |
| B | CYS422 |
| B | ILE423 |
| B | GLY424 |
| B | VNT502 |
| B | HOH604 |
| B | HOH620 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VNT B 502 |
| Chain | Residue |
| B | TYR103 |
| B | PHE105 |
| B | PHE110 |
| B | TYR116 |
| B | PRO210 |
| B | PHE290 |
| B | ALA291 |
| B | THR295 |
| B | LEU356 |
| B | MET360 |
| B | HEM501 |
| B | HOH805 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | TYR116 |
| C | ARG124 |
| C | LEU127 |
| C | LEU134 |
| C | ALA288 |
| C | ALA291 |
| C | GLY292 |
| C | THR295 |
| C | SER296 |
| C | ARG361 |
| C | GLY414 |
| C | PHE415 |
| C | GLY416 |
| C | VAL419 |
| C | HIS420 |
| C | CYS422 |
| C | ILE423 |
| C | GLY424 |
| C | VNT502 |
| C | HOH609 |
| C | HOH730 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VNT C 502 |
| Chain | Residue |
| C | LEU356 |
| C | MET360 |
| C | MET460 |
| C | HEM501 |
| C | HOH719 |
| C | TYR103 |
| C | PHE110 |
| C | TYR116 |
| C | PRO210 |
| C | VAL213 |
| C | PHE214 |
| C | PHE290 |
| C | ALA291 |
| C | THR295 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM D 501 |
| Chain | Residue |
| D | TYR116 |
| D | ARG124 |
| D | ALA288 |
| D | ALA291 |
| D | GLY292 |
| D | THR295 |
| D | SER296 |
| D | LEU359 |
| D | ARG361 |
| D | GLY414 |
| D | PHE415 |
| D | GLY416 |
| D | HIS420 |
| D | LYS421 |
| D | CYS422 |
| D | ILE423 |
| D | GLY424 |
| D | VNT502 |
| D | HOH602 |
| D | HOH661 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE VNT D 502 |
| Chain | Residue |
| D | TYR103 |
| D | PHE105 |
| D | PHE110 |
| D | TYR116 |
| D | PRO210 |
| D | PHE290 |
| D | ALA291 |
| D | THR295 |
| D | LEU356 |
| D | MET360 |
| D | MET460 |
| D | HEM501 |
| D | HOH714 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGVHKCIG |
| Chain | Residue | Details |
| A | PHE415-GLY424 |
