3GW9
Crystal structure of sterol 14-alpha demethylase (CYP51) from Trypanosoma brucei bound to an inhibitor N-(1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl)-4-(5-phenyl-1,3,4-oxaziazol-2-yl)benzamide
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 | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 480 |
| Chain | Residue |
| B | TYR116 |
| B | ARG361 |
| B | GLY414 |
| B | PHE415 |
| B | GLY416 |
| B | HIS420 |
| B | LYS421 |
| B | CYS422 |
| B | ILE423 |
| B | GLY424 |
| B | HOH481 |
| B | ARG124 |
| B | VNI490 |
| B | HOH495 |
| B | LEU134 |
| B | ALA288 |
| B | ALA291 |
| B | GLY292 |
| B | THR295 |
| B | THR299 |
| B | LEU356 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE VNI B 490 |
| Chain | Residue |
| B | PHE48 |
| B | TYR103 |
| B | PHE105 |
| B | PHE110 |
| B | TYR116 |
| B | PHE290 |
| B | ALA291 |
| B | THR295 |
| B | LEU356 |
| B | MET360 |
| B | HEM480 |
| B | HOH582 |
| B | HOH639 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM C 480 |
| Chain | Residue |
| C | TYR103 |
| C | TYR116 |
| C | ARG124 |
| C | LEU134 |
| C | ALA288 |
| C | ALA291 |
| C | GLY292 |
| C | THR295 |
| C | THR299 |
| C | LEU356 |
| C | ARG361 |
| C | GLY414 |
| C | PHE415 |
| C | GLY416 |
| C | HIS420 |
| C | LYS421 |
| C | CYS422 |
| C | ILE423 |
| C | GLY424 |
| C | VNI490 |
| C | HOH549 |
| C | HOH571 |
| C | HOH594 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE VNI C 490 |
| Chain | Residue |
| C | PHE48 |
| C | TYR103 |
| C | PHE105 |
| C | MET106 |
| C | PHE110 |
| C | TYR116 |
| C | PHE290 |
| C | ALA291 |
| C | THR295 |
| C | LEU356 |
| C | MET360 |
| C | MET460 |
| C | VAL461 |
| C | HEM480 |
| C | HOH572 |
| C | HOH638 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM D 480 |
| Chain | Residue |
| D | HOH5 |
| D | TYR116 |
| D | ARG124 |
| D | LEU127 |
| D | LEU134 |
| D | ALA288 |
| D | ALA291 |
| D | GLY292 |
| D | THR295 |
| D | THR299 |
| D | ARG361 |
| D | GLY414 |
| D | PHE415 |
| D | GLY416 |
| D | HIS420 |
| D | LYS421 |
| D | CYS422 |
| D | ILE423 |
| D | GLY424 |
| D | VNI490 |
| D | HOH535 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VNI D 490 |
| Chain | Residue |
| D | PHE214 |
| D | PHE290 |
| D | ALA291 |
| D | LEU356 |
| D | MET360 |
| D | MET460 |
| D | HEM480 |
| D | TYR103 |
| D | PHE110 |
| D | TYR116 |
| D | PRO210 |
| D | VAL213 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 480 |
| Chain | Residue |
| A | TYR116 |
| A | ARG124 |
| A | LEU127 |
| A | LEU134 |
| A | ALA288 |
| A | ALA291 |
| A | GLY292 |
| A | THR295 |
| A | THR299 |
| A | LEU356 |
| A | LEU359 |
| A | ARG361 |
| A | GLY414 |
| A | PHE415 |
| A | GLY416 |
| A | VAL419 |
| A | HIS420 |
| A | LYS421 |
| A | CYS422 |
| A | ILE423 |
| A | GLY424 |
| A | HOH483 |
| A | VNI490 |
| A | HOH592 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE VNI A 490 |
| Chain | Residue |
| A | PHE48 |
| A | TYR103 |
| A | PHE105 |
| A | PHE110 |
| A | TYR116 |
| A | PHE290 |
| A | ALA291 |
| A | THR295 |
| A | LEU356 |
| A | MET360 |
| A | MET460 |
| A | VAL461 |
| A | HEM480 |
| A | HOH495 |
| A | HOH566 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | HIS294 | |
| A | THR295 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| B | HIS294 | |
| B | THR295 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| C | HIS294 | |
| C | THR295 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| D | HIS294 | |
| D | THR295 |
