2X5L
X-RAY STRUCTURE OF THE SUBSTRATE-FREE MYCOBACTERIUM TUBERCULOSIS CYTOCHROME P450 CYP125, ALTERNATIVE CRYSTAL FORM
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 | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 1434 |
| Chain | Residue |
| A | MET116 |
| A | SER276 |
| A | PRO312 |
| A | PHE316 |
| A | ARG318 |
| A | GLY368 |
| A | PHE369 |
| A | GLY370 |
| A | HIS375 |
| A | TYR376 |
| A | CYS377 |
| A | LEU117 |
| A | ILE378 |
| A | HOH2517 |
| A | HOH2593 |
| A | HOH2712 |
| A | HOH2713 |
| A | HIS124 |
| A | ARG128 |
| A | MET264 |
| A | ALA268 |
| A | GLY269 |
| A | THR272 |
| A | THR273 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19846552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IW1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20545858","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2X5L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XC3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XN8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IVY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IW0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IW1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IW2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
