5te8

X-ray diffraction
2.7Å resolution

Crystal structure of the midazolam-bound human CYP3A4

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for regiospecific midazolam oxidation by human cytochrome P450 3A4.
Proc Natl Acad Sci U S A 114 486-491 (2017)
PMID: 28031486

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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 3A4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 487 amino acids
Theoretical weight: 55.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 3 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 64.289Å b: 117.98Å c: 205.649Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.224 0.292
Expression system: Escherichia coli BL21(DE3)