› 5a4k

X-ray diffraction
2.09Å resolution

Crystal structure of the R139W variant of human NAD(P)H:quinone oxidoreductase

Released:
DOI: 10.2210/pdb5a4k/pdb
PDB entry 5a4k coloured by chain, front view.
PDB entry 5a4k coloured by chain, side view.
PDB entry 5a4k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1).
Lienhart WD, Strandback E, Gudipati V, Koch K, Binter A, Uhl MK, Rantasa DM, Bourgeois B, Madl T, Zangger K, Gruber K, Macheroux P
FEBS J 284 1233-1245 (2017)
PMID: 28236663

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 294 amino acids
Theoretical weight: 33.11 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 4 x FAD
1 bound ligand:
Ligand BTB 2 x BTB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 54.606Å b: 56.928Å c: 99.827Å
α: 100.37° β: 92.85° γ: 90.22°
R-values:
R R work R free
0.171 0.169 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 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)
4 more

1 mention without citation

Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1).
Lienhart et al. (2017)