PDBe 1qbg

X-ray diffraction
2.3Å resolution

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

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: NEW 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