5LIE
Crystal structure of Mycobacterium tuberculosis CYP126A1 in complex with imidazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase activity |
| 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| 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 501 |
| Chain | Residue |
| A | LEU95 |
| A | ARG305 |
| A | GLY355 |
| A | PHE356 |
| A | GLY357 |
| A | HIS361 |
| A | CYS363 |
| A | GLY365 |
| A | ALA369 |
| A | IMD502 |
| A | HOH655 |
| A | ASN96 |
| A | HOH657 |
| A | HOH789 |
| A | HIS103 |
| A | ARG107 |
| A | MET157 |
| A | ALA253 |
| A | THR257 |
| A | THR258 |
| A | LYS303 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue IMD A 502 |
| Chain | Residue |
| A | LEU249 |
| A | ALA253 |
| A | THR257 |
| A | HEM501 |
| A | HOH608 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LEU95 |
| B | ASN96 |
| B | HIS103 |
| B | ARG107 |
| B | MET157 |
| B | ILE158 |
| B | LEU161 |
| B | ALA253 |
| B | GLY254 |
| B | THR257 |
| B | THR258 |
| B | SER261 |
| B | LYS303 |
| B | ARG305 |
| B | GLY355 |
| B | PHE356 |
| B | GLY357 |
| B | HIS361 |
| B | CYS363 |
| B | GLY365 |
| B | LEU368 |
| B | ALA369 |
| B | HOH604 |
| B | HOH662 |
| B | HOH702 |
| B | HOH770 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGqGVHYCLG |
| Chain | Residue | Details |
| A | PHE356-GLY365 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
