6FMO
Crystal structure of the substrate (obtusifoliol)-bound and ligand-free I105F mutant of sterol 14-alpha demethylase (CYP51) from Trypanosoma cruzi
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008398 | molecular_function | sterol 14-demethylase 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 | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008398 | molecular_function | sterol 14-demethylase 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 | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0008398 | molecular_function | sterol 14-demethylase activity |
| C | 0016020 | cellular_component | membrane |
| C | 0016126 | biological_process | sterol biosynthetic process |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0008398 | molecular_function | sterol 14-demethylase activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016126 | biological_process | sterol biosynthetic process |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 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 501 |
| Chain | Residue |
| A | TYR103 |
| A | GLY414 |
| A | HIS420 |
| A | CYS422 |
| A | ILE423 |
| A | GLY424 |
| A | TYR116 |
| A | LEU127 |
| A | ALA291 |
| A | THR295 |
| A | THR299 |
| A | LEU356 |
| A | VAL359 |
| A | ARG361 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue DVE A 502 |
| Chain | Residue |
| A | TYR103 |
| A | MET106 |
| A | TYR116 |
| A | GLN126 |
| A | MET284 |
| A | ALA287 |
| A | ALA288 |
| A | ALA291 |
| A | MET358 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | TYR103 |
| B | TYR116 |
| B | LEU127 |
| B | ALA291 |
| B | THR295 |
| B | THR299 |
| B | VAL359 |
| B | ARG361 |
| B | GLY414 |
| B | PHE415 |
| B | HIS420 |
| B | CYS422 |
| B | ILE423 |
| B | GLY424 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue DVE B 502 |
| Chain | Residue |
| B | TYR103 |
| B | PHE110 |
| B | TYR116 |
| B | ALA288 |
| B | ALA291 |
| B | MET358 |
| B | MET460 |
| B | VAL461 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue HEM C 501 |
| Chain | Residue |
| C | TYR103 |
| C | TYR116 |
| C | LEU127 |
| C | ALA291 |
| C | THR295 |
| C | THR299 |
| C | LEU356 |
| C | VAL359 |
| C | ARG361 |
| C | GLY414 |
| C | PHE415 |
| C | GLY416 |
| C | HIS420 |
| C | CYS422 |
| C | GLY424 |
| C | DVE502 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue DVE C 502 |
| Chain | Residue |
| C | TYR103 |
| C | PHE105 |
| C | TYR116 |
| C | MET284 |
| C | ALA287 |
| C | ALA288 |
| C | MET358 |
| C | MET460 |
| C | HEM501 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue HEM D 501 |
| Chain | Residue |
| D | TYR103 |
| D | TYR116 |
| D | ARG124 |
| D | ALA288 |
| D | ALA291 |
| D | GLY292 |
| D | THR295 |
| D | THR299 |
| D | VAL359 |
| D | ARG361 |
| D | GLY414 |
| D | PHE415 |
| D | GLY416 |
| D | HIS420 |
| D | CYS422 |
| D | ILE423 |
| D | GLY424 |
| D | ALA428 |
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 | 80 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | MET1-VAL21 | |
| B | MET1-VAL21 | |
| C | MET1-VAL21 | |
| D | MET1-VAL21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:P0A512 |
| Chain | Residue | Details |
| A | CYS422 | |
| B | CYS422 | |
| C | CYS422 | |
| D | CYS422 |
