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 | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0007032 | biological_process | endosome organization |
| A | 0008202 | biological_process | steroid metabolic process |
| 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 | 0071466 | biological_process | cellular response to xenobiotic stimulus |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5TZ1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5V5Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5FSA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PDB","id":"5FSA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5V5Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
