5vc0

X-ray diffraction
2.7Å resolution

Crystal structure of human CYP3A4 bound to ritonavir

Released:
Source organism: Homo sapiens
Primary publication:
High-Level Production and Properties of the Cysteine-Depleted Cytochrome P450 3A4.
Biochemistry 56 3058-3067 (2017)
PMID: 28590129

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-140290 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 3A4 Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 55.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08684 (Residues: 21-503; Coverage: 96%)
Gene names: CYP3A3, CYP3A4
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: I222
Unit cell:
a: 76.579Å b: 100.069Å c: 125.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.208 0.283
Expression system: Escherichia coli