Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7P5T

Structure of CYP142 from Mycobacterium tuberculosis in complex with inhibitor MEK216

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006629biological_processlipid metabolic process
A0006707biological_processcholesterol catabolic process
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0009274cellular_componentpeptidoglycan-based cell wall
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0031073molecular_functioncholesterol 26-hydroxylase activity
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGTHFCLG
ChainResidueDetails
APHE333-GLY342

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20889498","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XKR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon