› 1qbg

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF HUMAN DT-DIAPHORASE (NAD(P)H OXIDOREDUCTASE)

Released:
DOI: 10.2210/pdb1qbg/pdb
PDB entry 1qbg coloured by chain, front view.
PDB entry 1qbg coloured by chain, side view.
PDB entry 1qbg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).
Skelly JV, Sanderson MR, Suter DA, Baumann U, Read MA, Gregory DS, Bennett M, Hobbs SM, Neidle S
J Med Chem 42 4325-30 (1999)
PMID: 10543876

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-147404 (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: 272 amino acids
Theoretical weight: 30.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15559 (Residues: 3-274; Coverage: 99%)
Gene names: DIA4, 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 RU200
Spacegroup: P1
Unit cell:
a: 55.88Å b: 57.49Å c: 98.77Å
α: 77.1° β: 76.2° γ: 86.9°
R-values:
R R work R free
0.238 not available 0.28
Expression system: Escherichia coli

Quick links

Citations

3 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)
2 more

8 mentions without citation

Deamidation of human proteins.
Robinson et al. (2001)
7 more