2v0m

X-ray diffraction
2.8Å resolution

Crystal structure of human P450 3A4 in complex with ketoconazole

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for ligand promiscuity in cytochrome P450 3A4.
Proc Natl Acad Sci U S A 103 13682-7 (2006)
PMID: 16954191

Function and Biology Details

Reactions catalysed:
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
Quinine + [reduced NADPH--hemoprotein reductase] + O(2) = 3-hydroxyquinine + [oxidized NADPH--hemoprotein reductase] + H(2)O
1,8-cineole + [reduced NADPH--hemoprotein reductase] + O(2) = 2-exo-hydroxy-1,8-cineole + [oxidized NADPH--hemoprotein reductase] + H(2)O
Albendazole + [reduced NADPH--hemoprotein reductase] + O(2) = albendazole S-oxide + [oxidized NADPH--hemoprotein reductase] + H(2)O

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 3A4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 485 amino acids
Theoretical weight: 55.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08684 (Residues: 25-503; Coverage: 95%)
Gene names: CYP3A3, CYP3A4
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 228.942Å b: 66.363Å c: 146.419Å
α: 90° β: 102.8° γ: 90°
R-values:
R R work R free
0.22 0.218 0.271
Expression system: Escherichia coli