5HDI
Structural characterization of CYP144A1, a Mycobacterium tuberculosis cytochrome P450
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 | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 | 24 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | LEU121 |
| A | HIS325 |
| A | ARG327 |
| A | SER378 |
| A | PHE379 |
| A | GLY380 |
| A | ALA383 |
| A | HIS384 |
| A | CYS386 |
| A | VAL387 |
| A | GLY388 |
| A | ALA122 |
| A | ALA392 |
| A | HOH615 |
| A | HOH628 |
| A | HOH680 |
| A | HOH681 |
| A | HIS129 |
| A | ARG133 |
| A | ALA275 |
| A | GLY276 |
| A | SER279 |
| A | THR280 |
| A | PHE322 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LEU121 |
| B | ALA122 |
| B | HIS129 |
| B | ARG133 |
| B | ALA275 |
| B | GLY276 |
| B | SER279 |
| B | THR280 |
| B | PHE322 |
| B | HIS325 |
| B | ARG327 |
| B | SER378 |
| B | PHE379 |
| B | GLY380 |
| B | ALA383 |
| B | HIS384 |
| B | CYS386 |
| B | VAL387 |
| B | GLY388 |
| B | ALA392 |
| B | HOH620 |
| B | HOH631 |
| B | HOH687 |
| B | HOH693 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGkGAHFCVG |
| Chain | Residue | Details |
| A | PHE379-GLY388 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
