5V5Z
Structure of CYP51 from the pathogen Candida albicans
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001766 | biological_process | membrane raft polarization |
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 | 0005886 | cellular_component | plasma membrane |
A | 0006696 | biological_process | ergosterol biosynthetic process |
A | 0007032 | biological_process | endosome organization |
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 | 0032541 | cellular_component | cortical endoplasmic reticulum |
A | 0036187 | biological_process | cell growth mode switching, budding to filamentous |
A | 0046872 | molecular_function | metal ion binding |
A | 0097038 | cellular_component | perinuclear endoplasmic reticulum |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue HEM A 601 |
Chain | Residue |
A | PHE105 |
A | ILE379 |
A | ARG381 |
A | PRO462 |
A | PHE463 |
A | HIS468 |
A | CYS470 |
A | ILE471 |
A | 1YN602 |
A | TYR118 |
A | TYR132 |
A | LEU139 |
A | LYS143 |
A | ILE304 |
A | GLY308 |
A | THR311 |
A | PRO375 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue 1YN A 602 |
Chain | Residue |
A | ALA61 |
A | TYR118 |
A | ILE131 |
A | TYR132 |
A | PRO230 |
A | PHE233 |
A | GLY303 |
A | ILE304 |
A | GLY307 |
A | THR311 |
A | LEU376 |
A | HIS377 |
A | SER378 |
A | PHE380 |
A | TYR505 |
A | SER506 |
A | MET508 |
A | 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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | LEU15-TRP37 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:5TZ1 |
Chain | Residue | Details |
A | TYR64 | |
A | HIS377 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:5V5Z |
Chain | Residue | Details |
A | TYR118 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:5FSA |
Chain | Residue | Details |
A | GLY307 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0007744|PDB:5FSA, ECO:0007744|PDB:5TZ1, ECO:0007744|PDB:5V5Z |
Chain | Residue | Details |
A | CYS470 |