8S4M
Crystal structure of Mycobacterium tuberculosis cytochrome P450 CYP125 in complex with an inhibitor
This is a non-PDB format compatible entry.
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 |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006707 | biological_process | cholesterol catabolic process |
B | 0008202 | biological_process | steroid metabolic process |
B | 0008203 | biological_process | cholesterol metabolic process |
B | 0008395 | molecular_function | steroid hydroxylase activity |
B | 0016042 | biological_process | lipid catabolic process |
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 |
B | 0051701 | biological_process | biological process involved in interaction with host |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006707 | biological_process | cholesterol catabolic process |
C | 0008202 | biological_process | steroid metabolic process |
C | 0008203 | biological_process | cholesterol metabolic process |
C | 0008395 | molecular_function | steroid hydroxylase activity |
C | 0016042 | biological_process | lipid catabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
C | 0020037 | molecular_function | heme binding |
C | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051701 | biological_process | biological process involved in interaction with host |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
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 | 3 |
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 |