› 1qrd

X-ray diffraction
2.4Å resolution

QUINONE REDUCTASE/FAD/CIBACRON BLUE/DUROQUINONE COMPLEX

Released:
DOI: 10.2210/pdb1qrd/pdb
PDB entry 1qrd coloured by chain, front view.
PDB entry 1qrd coloured by chain, side view.
PDB entry 1qrd coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.
Li R, Bianchet MA, Talalay P, Amzel LM
Proc Natl Acad Sci U S A 92 8846-50 (1995)
PMID: 7568029

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-138849 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD(P)H dehydrogenase [quinone] 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 273 amino acids
Theoretical weight: 30.85 KDa
Source organism: Rattus rattus
UniProt:
  • Canonical: P05982 (Residues: 2-274; Coverage: 100%)
Gene names: Nmor1, Nqo1
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand CBD 2 x CBD
Ligand DQN 2 x DQN
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 72Å b: 107Å c: 88.4Å
α: 90° β: 92.6° γ: 90°
R-values:
R R work R free
0.188 0.188 not available

Quick links

Citations

37 review citations

NAD(P)H:quinone oxidoreductase 1 (NQO1): chemoprotection, bioactivation, gene regulation and genetic polymorphisms.
Ross et al. (2000)
36 more

8 mentions without citation

Principles and characteristics of biological assemblies in experimentally determined protein structures.
Xu et al. (2019)
7 more