2X5W
X-ray structure of Mycobacterium tuberculosis cytochrome P450 CYP125 in complex with substrate cholest-4-en-3-one
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 | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0016042 | biological_process | lipid catabolic 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051701 | biological_process | biological process involved in interaction with host |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1428 |
| Chain | Residue |
| A | ARG84 |
| A | HIS85 |
| A | HIS195 |
| A | ASN198 |
| A | TYR208 |
| A | HOH2226 |
| A | HOH2239 |
| A | HOH2432 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE K2B A 1429 |
| Chain | Residue |
| A | GLN112 |
| A | MET200 |
| A | PRO213 |
| A | LYS214 |
| A | VAL267 |
| A | ALA268 |
| A | TRP414 |
| A | HEM1431 |
| A | HOH2434 |
| A | ASP108 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1430 |
| Chain | Residue |
| A | HIS210 |
| A | TYR376 |
| A | ALA380 |
| A | ASN381 |
| A | ARG384 |
| A | HOH2388 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 1431 |
| Chain | Residue |
| A | MET116 |
| A | LEU117 |
| A | HIS124 |
| A | ARG128 |
| A | ILE179 |
| A | MET264 |
| A | ALA268 |
| A | THR272 |
| A | THR273 |
| A | PRO312 |
| A | PHE316 |
| A | ARG318 |
| A | GLY368 |
| A | PHE369 |
| A | GLY370 |
| A | HIS375 |
| A | CYS377 |
| A | ILE378 |
| A | GLY379 |
| A | ALA383 |
| A | K2B1429 |
| A | HOH2344 |
| A | HOH2436 |
| A | HOH2437 |
| A | HOH2438 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19846552, ECO:0007744|PDB:3IW1 |
| Chain | Residue | Details |
| A | GLY202 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:20545858, ECO:0007744|PDB:2X5L, ECO:0007744|PDB:2X5W, ECO:0007744|PDB:2XC3, ECO:0007744|PDB:2XN8, ECO:0007744|PDB:3IVY, ECO:0007744|PDB:3IW0, ECO:0007744|PDB:3IW1, ECO:0007744|PDB:3IW2 |
| Chain | Residue | Details |
| A | CYS377 |
