1og2

X-ray diffraction
2.6Å resolution

Structure of human cytochrome P450 CYP2C9

Released:

Function and Biology Details

Reactions catalysed:
(S)-limonene + [reduced NADPH--hemoprotein reductase] + O(2) = (-)-perillyl alcohol + [oxidized NADPH--hemoprotein reductase] + H(2)O
(+)-(R)-limonene + [reduced NADPH--hemoprotein reductase] + O(2) = (+)-trans-carveol + [oxidized NADPH--hemoprotein reductase] + H(2)O
(S)-limonene + [reduced NADPH--hemoprotein reductase] + O(2) = (-)-trans-carveol + [oxidized NADPH--hemoprotein reductase] + H(2)O
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 2C9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 475 amino acids
Theoretical weight: 54.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11712 (Residues: 19-490; Coverage: 96%)
Gene names: CYP2C10, CYP2C9
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEC 2 x HEC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P321
Unit cell:
a: 164.87Å b: 164.87Å c: 111.105Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.208 0.259
Expression system: Escherichia coli