PDBe 1d4a

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION

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

Assembly composition:
homo dimer (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: 273 amino acids
Theoretical weight: 30.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15559 (Residues: 2-274; Coverage: 100%)
Gene names: DIA4, NMOR1, NQO1
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 55.678Å b: 57.032Å c: 97.402Å
α: 77.04° β: 76.72° γ: 86.89°
R-values:
R R work R free
0.209 0.209 0.253
Expression system: Escherichia coli