4UYM
Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with voriconazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008398 | molecular_function | sterol 14-demethylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016126 | biological_process | sterol biosynthetic 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 | 0032259 | biological_process | methylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006696 | biological_process | ergosterol biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008398 | molecular_function | sterol 14-demethylase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016126 | biological_process | sterol biosynthetic 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 | 0032259 | biological_process | methylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 580 |
| Chain | Residue |
| A | TYR136 |
| A | PHE456 |
| A | HIS461 |
| A | CYS463 |
| A | VOR590 |
| A | HOH2078 |
| A | LEU143 |
| A | LYS147 |
| A | LEU304 |
| A | GLY308 |
| A | SER311 |
| A | ILE376 |
| A | ARG378 |
| A | PRO455 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE VOR A 590 |
| Chain | Residue |
| A | TYR122 |
| A | PHE130 |
| A | ILE373 |
| A | SER375 |
| A | LEU503 |
| A | PHE504 |
| A | HEM580 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM B 580 |
| Chain | Residue |
| B | TYR136 |
| B | LYS147 |
| B | LEU304 |
| B | GLY308 |
| B | SER311 |
| B | ILE376 |
| B | ARG378 |
| B | PRO455 |
| B | PHE456 |
| B | GLY457 |
| B | HIS461 |
| B | CYS463 |
| B | ILE464 |
| B | GLY465 |
| B | VOR590 |
| B | HOH2069 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE VOR B 590 |
| Chain | Residue |
| B | TYR122 |
| B | PHE130 |
| B | TYR136 |
| B | ILE373 |
| B | SER375 |
| B | LEU503 |
| B | PHE504 |
| B | HEM580 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGRHRCIG |
| Chain | Residue | Details |
| A | PHE456-GLY465 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0007744|PDB:4UYL, ECO:0007744|PDB:4UYM, ECO:0007744|PDB:5FRB |
| Chain | Residue | Details |
| A | CYS463 | |
| B | CYS463 |
