3IW1
Crystal structure of Mycobacterium tuberculosis cytochrome P450 CYP125 in complex with androstenedione
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 | 7 |
| Details | BINDING SITE FOR RESIDUE ASD A 1223 |
| Chain | Residue |
| A | VAL111 |
| A | MET200 |
| A | GLY202 |
| A | SER217 |
| A | VAL297 |
| A | HOH561 |
| A | HOH579 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 434 |
| Chain | Residue |
| A | ARG128 |
| A | PHE135 |
| A | MET264 |
| A | ALA268 |
| A | GLY269 |
| A | THR272 |
| A | THR273 |
| A | PRO312 |
| A | PHE316 |
| A | ARG318 |
| A | GLY368 |
| A | PHE369 |
| A | GLY370 |
| A | GLY371 |
| A | HIS375 |
| A | CYS377 |
| A | ILE378 |
| A | GLY379 |
| A | HOH459 |
| A | HOH466 |
| A | HOH531 |
| A | HOH601 |
| A | LEU117 |
| A | HIS124 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1akd |
| Chain | Residue | Details |
| A | THR272 | |
| A | GLU271 |
