› 4cf6

X-ray diffraction
2.69Å resolution

Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with Cibacron blue at 2.7 A resolution

Released:
DOI: 10.2210/pdb4cf6/pdb
PDB entry 4cf6 coloured by chain, front view.
PDB entry 4cf6 coloured by chain, side view.
PDB entry 4cf6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Collapse of the native structure caused by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase(1.).
Lienhart WD, Gudipati V, Uhl MK, Binter A, Pulido SA, Saf R, Zangger K, Gruber K, Macheroux P
FEBS J 281 4691-4704 (2014)
PMID: 25143260

Function and Biology Details

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

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
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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 2 x FAD
1 bound ligand:
Ligand CBD 2 x CBD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 104.167Å b: 104.563Å c: 118.566Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.185 0.207
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

Functions of NQO1 in Cellular Protection and CoQ10 Metabolism and its Potential Role as a Redox Sensitive Molecular Switch.
Ross et al. (2017)
5 more

3 mentions without citation

NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just enough mobility, in just the right places.
Pey et al. (2019)
2 more