› 1dxq

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF MOUSE NAD[P]H-QUINONE OXIDOREDUCTASE

Released:
DOI: 10.2210/pdb1dxq/pdb
PDB entry 1dxq coloured by chain, front view.
PDB entry 1dxq coloured by chain, side view.
PDB entry 1dxq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
Faig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM
Proc Natl Acad Sci U S A 97 3177-82 (2000)
PMID: 10706635

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179151 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H dehydrogenase [quinone] 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 273 amino acids
Theoretical weight: 30.85 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64669 (Residues: 2-274; Coverage: 100%)
Gene names: Dia4, Nmo1, Nmor1, Nqo1
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 54.96Å b: 171.62Å c: 67.14Å
α: 90° β: 112.3° γ: 90°
R-values:
R R work R free
0.207 0.207 0.277
Expression system: Escherichia coli

Quick links

Citations

22 review citations

NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1), a multifunctional antioxidant enzyme and exceptionally versatile cytoprotector.
Dinkova-Kostova et al. (2010)
21 more

2 mentions without citation

Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
Faig et al. (2000)
1 more