X-ray diffraction
2.4Å resolution

Crystal Structure of Human NADPH-Cytochrome P450 Reductase (R457H Mutant)

Source organism: Homo sapiens
Primary publication:
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency.
Proc. Natl. Acad. Sci. U.S.A. 108 13486-91 (2011)
PMID: 21808038

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
NADPH--cytochrome P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 618 amino acids
Theoretical weight: 70.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P16435 (Residues: 64-677; Coverage: 91%)
Gene names: CYPOR, POR
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand FMN 2 x FMN

Cofactor: Ligand NAP 2 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 70.276Å b: 120.393Å c: 156.345Å
α: 90° β: 90° γ: 90°
R R work R free
0.227 0.227 0.285
Expression system: Escherichia coli