› 5fuq

X-ray diffraction
2.04Å resolution

CRYSTAL STRUCTURE OF THE H80R VARIANT OF NQO1 BOUND TO DICOUMAROL

Released:
DOI: 10.2210/pdb5fuq/pdb
PDB entry 5fuq coloured by chain, front view.
PDB entry 5fuq coloured by chain, side view.
PDB entry 5fuq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Enhanced vulnerability of human proteins towards disease-associated inactivation through divergent evolution.
Medina-Carmona E, Fuchs JE, Gavira JA, Mesa-Torres N, Neira JL, Salido E, Palomino-Morales R, Burgos M, Timson DJ, Pey AL
Hum Mol Genet 26 3531-3544 (2017)
PMID: 28911204

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: 274 amino acids
Theoretical weight: 30.93 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 2 x FAD
2 bound ligands:
Ligand DTC 3 x DTC
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 104.828Å b: 104.828Å c: 201.908Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.177
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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