› 1dxo

X-ray diffraction
2.5Å resolution

Crystal structure of human NAD[P]H-QUINONE oxidoreductase CO with 2,3,5,6,tetramethyl-P-benzoquinone (duroquinone) at 2.5 Angstrom resolution

Released:
DOI: 10.2210/pdb1dxo/pdb
PDB entry 1dxo coloured by chain, front view.
PDB entry 1dxo coloured by chain, side view.
PDB entry 1dxo coloured by chain, top view.
Source organism: Homo sapiens
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-147405 (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: 30.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15559 (Residues: 2-274; Coverage: 100%)
Gene names: DIA4, NMOR1, NQO1
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand DQN 4 x DQN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P1
Unit cell:
a: 55.579Å b: 56.912Å c: 97.755Å
α: 76.24° β: 76.73° γ: 86.33°
R-values:
R R work R free
0.202 0.202 0.264
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

8 mentions without citation

Insufficiently dehydrated hydrogen bonds as determinants of protein interactions.
Fernández et al. (2003)
7 more