X-ray diffraction
3Å resolution

A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases.


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: 682 amino acids
Theoretical weight: 75.84 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
  • Canonical: P16603 (Residues: 24-691; Coverage: 97%)
Gene names: CPR1, NCP1, NCPR1, PRD1, YHR042W
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand FMN 4 x FMN

Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NAP 2 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 77.751Å b: 87.094Å c: 259.59Å
α: 90° β: 90° γ: 90°
R R work R free
0.197 0.197 0.261
Expression system: Escherichia coli