4C28
Crystal structure of Trypanosoma cruzi CYP51 bound to the inhibitor (R)-N-(3-(1H-indol-3-yl)-1-oxo-1-(pyridin-4-ylamino)propan-2-yl)-4-(4-(4-chlorophenyl)piperazin-1-yl)-2-fluorobenzamide.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0006699 | biological_process | bile acid biosynthetic process |
A | 0008387 | molecular_function | steroid 7-alpha-hydroxylase activity |
A | 0008396 | molecular_function | oxysterol 7-alpha-hydroxylase activity |
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 | 0042632 | biological_process | cholesterol homeostasis |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0006699 | biological_process | bile acid biosynthetic process |
B | 0008387 | molecular_function | steroid 7-alpha-hydroxylase activity |
B | 0008396 | molecular_function | oxysterol 7-alpha-hydroxylase activity |
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 | 0042632 | biological_process | cholesterol homeostasis |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM A 1450 |
Chain | Residue |
A | TYR116 |
A | LEU356 |
A | ARG361 |
A | GLY414 |
A | PHE415 |
A | GLY416 |
A | VAL419 |
A | HIS420 |
A | LYS421 |
A | CYS422 |
A | ILE423 |
A | ARG124 |
A | GLY424 |
A | TW51460 |
A | HOH2052 |
A | HOH2201 |
A | LEU127 |
A | LEU134 |
A | ALA288 |
A | ALA291 |
A | GLY292 |
A | THR295 |
A | THR299 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE TW5 A 1460 |
Chain | Residue |
A | ILE45 |
A | PHE48 |
A | GLY49 |
A | PHE110 |
A | TYR116 |
A | PRO210 |
A | PHE214 |
A | PHE290 |
A | ALA291 |
A | LEU356 |
A | MET460 |
A | VAL461 |
A | HEM1450 |
A | HOH2050 |
A | HOH2101 |
B | PRO222 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 1450 |
Chain | Residue |
B | MET123 |
B | ARG124 |
B | LEU134 |
B | ALA288 |
B | ALA291 |
B | GLY292 |
B | THR295 |
B | SER296 |
B | LEU356 |
B | VAL359 |
B | ARG361 |
B | GLY414 |
B | PHE415 |
B | GLY416 |
B | HIS420 |
B | CYS422 |
B | ILE423 |
B | GLY424 |
B | ALA428 |
B | TW51460 |
B | HOH2154 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TW5 B 1460 |
Chain | Residue |
A | PRO222 |
B | ILE45 |
B | PHE48 |
B | MET106 |
B | PHE110 |
B | TYR116 |
B | PRO210 |
B | PHE214 |
B | ALA291 |
B | MET460 |
B | VAL461 |
B | HEM1450 |
B | HOH2073 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1478 |
Chain | Residue |
A | ILE175 |
A | ALA179 |
A | ALA288 |
A | MET289 |
A | GLY292 |
A | GLN293 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 1479 |
Chain | Residue |
A | GLY111 |
A | GLU112 |
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 |