5EAF
Saccharomyces cerevisiae CYP51 complexed with the plant pathogen inhibitor Fluquinconazole
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0016020 | cellular_component | membrane |
A | 0016126 | biological_process | sterol biosynthetic process |
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 | 0008168 | molecular_function | methyltransferase activity |
B | 0016020 | cellular_component | membrane |
B | 0016126 | biological_process | sterol biosynthetic process |
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 | 20 |
Details | binding site for residue HEM A 601 |
Chain | Residue |
A | PHE113 |
A | LEU374 |
A | PRO379 |
A | LEU383 |
A | ARG385 |
A | PRO462 |
A | PHE463 |
A | GLY464 |
A | HIS468 |
A | CYS470 |
A | GLY472 |
A | TYR126 |
A | FQC602 |
A | TYR140 |
A | LEU147 |
A | LYS151 |
A | VAL311 |
A | GLY315 |
A | THR318 |
A | THR322 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue FQC A 602 |
Chain | Residue |
A | TYR126 |
A | LEU129 |
A | THR130 |
A | ILE139 |
A | GLY310 |
A | GLY314 |
A | LEU380 |
A | HEM601 |
site_id | AC3 |
Number of Residues | 21 |
Details | binding site for residue HEM B 601 |
Chain | Residue |
B | PHE113 |
B | TYR126 |
B | TYR140 |
B | LEU147 |
B | LYS151 |
B | VAL311 |
B | GLY315 |
B | THR318 |
B | THR322 |
B | LEU374 |
B | PRO379 |
B | LEU383 |
B | ARG385 |
B | PRO462 |
B | PHE463 |
B | GLY464 |
B | HIS468 |
B | ARG469 |
B | CYS470 |
B | GLY472 |
B | FQC602 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue FQC B 602 |
Chain | Residue |
B | TYR126 |
B | THR130 |
B | PHE134 |
B | PHE236 |
B | PHE241 |
B | GLY310 |
B | GLY314 |
B | LEU380 |
B | HEM601 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGRHRCIG |
Chain | Residue | Details |
A | PHE463-GLY472 |