4COH
Crystal structure of Trypanosoma cruzi CYP51 bound to the sulfonamide derivative of the 4-aminopyridyl-based inhibitor
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 | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 1450 |
| Chain | Residue |
| A | TYR116 |
| A | GLY414 |
| A | PHE415 |
| A | GLY416 |
| A | HIS420 |
| A | CYS422 |
| A | ILE423 |
| A | GLY424 |
| A | T9H1460 |
| A | HOH2076 |
| A | HOH2307 |
| A | ALA288 |
| A | HOH2310 |
| A | HOH2362 |
| A | ALA291 |
| A | GLY292 |
| A | THR295 |
| A | THR299 |
| A | LEU356 |
| A | VAL359 |
| A | ARG361 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE T9H A 1460 |
| Chain | Residue |
| A | PHE48 |
| A | TYR103 |
| A | MET106 |
| A | PHE110 |
| A | TYR116 |
| A | PRO210 |
| A | ALA211 |
| A | PHE214 |
| A | ALA291 |
| A | LEU356 |
| A | MET460 |
| A | VAL461 |
| A | HEM1450 |
| A | HOH2011 |
| A | HOH2225 |
| A | HOH2363 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 1450 |
| Chain | Residue |
| B | TYR116 |
| B | LEU134 |
| B | ALA288 |
| B | ALA291 |
| B | THR295 |
| B | VAL359 |
| B | ARG361 |
| B | GLY414 |
| B | PHE415 |
| B | GLY416 |
| B | HIS420 |
| B | CYS422 |
| B | ILE423 |
| B | GLY424 |
| B | T9H1460 |
| B | HOH2088 |
| B | HOH2278 |
| B | HOH2313 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE T9H B 1460 |
| Chain | Residue |
| A | PRO222 |
| B | PHE48 |
| B | PHE110 |
| B | TYR116 |
| B | PRO210 |
| B | PHE214 |
| B | ALA287 |
| B | PHE290 |
| B | ALA291 |
| B | MET460 |
| B | VAL461 |
| B | HEM1450 |
| B | HOH2011 |
| B | HOH2067 |
| B | HOH2252 |
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: axial binding residue => ECO:0000250|UniProtKB:P0A512 |
| Chain | Residue | Details |
| A | CYS422 | |
| B | CYS422 |
