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 |