4CK8
STEROL 14-ALPHA DEMETHYLASE (CYP51)FROM TRYPANOSOMA CRUZI IN COMPLEX WITH (R)-1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl 4-(4-(3,4- dichlorophenyl)piperazin-1-yl)phenylcarbamate (LFD)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0008202 | biological_process | steroid metabolic process |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 1480 |
| Chain | Residue |
| A | TYR103 |
| A | GLY414 |
| A | PHE415 |
| A | GLY416 |
| A | HIS420 |
| A | LYS421 |
| A | CYS422 |
| A | GLY424 |
| A | LFD1490 |
| A | ALA288 |
| A | ALA291 |
| A | GLY292 |
| A | THR295 |
| A | THR299 |
| A | LEU356 |
| A | VAL359 |
| A | ARG361 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LFD A 1490 |
| Chain | Residue |
| A | ILE45 |
| A | PHE48 |
| A | PHE110 |
| A | TYR116 |
| A | PRO210 |
| A | VAL213 |
| A | PHE290 |
| A | ALA291 |
| A | THR295 |
| A | MET460 |
| A | HEM1480 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 1480 |
| Chain | Residue |
| B | TYR103 |
| B | ARG124 |
| B | LEU127 |
| B | ALA288 |
| B | ALA291 |
| B | GLY292 |
| B | THR295 |
| B | THR299 |
| B | LEU356 |
| B | VAL359 |
| B | ARG361 |
| B | GLY414 |
| B | PHE415 |
| B | GLY416 |
| B | HIS420 |
| B | CYS422 |
| B | ILE423 |
| B | GLY424 |
| B | LFD1490 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LFD B 1490 |
| Chain | Residue |
| B | ILE45 |
| B | GLY49 |
| B | TYR103 |
| B | PHE110 |
| B | TYR116 |
| B | PRO210 |
| B | PHE290 |
| B | ALA291 |
| B | THR295 |
| B | LEU356 |
| B | MET460 |
| B | HEM1480 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P0A512","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
