4cet

X-ray diffraction
2.2Å resolution

Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with dicoumarol at 2.2 A resolution

Released:

Function and Biology Details

Reaction catalysed:
NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H dehydrogenase [quinone] 1 Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15559 (Residues: 1-274; Coverage: 100%)
Gene names: DIA4, NMOR1, NQO1
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P41212
Unit cell:
a: 51.05Å b: 51.05Å c: 169.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.224
Expression system: Escherichia coli BL21(DE3)