› 1gg5

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AND A CHEMOTHERAPEUTIC DRUG (E09) AT 2.5 A RESOLUTION

Released:
DOI: 10.2210/pdb1gg5/pdb
PDB entry 1gg5 coloured by chain, front view.
PDB entry 1gg5 coloured by chain, side view.
PDB entry 1gg5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.
Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM
Structure 9 659-67 (2001)
PMID: 11587640

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

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: 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


Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand E09 4 x E09
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 56.733Å b: 55.454Å c: 97.205Å
α: 76.42° β: 77.22° γ: 86.45°
R-values:
R R work R free
0.2 0.2 0.279
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Implications of protein flexibility for drug discovery.
Teague SJ. (2003)
4 more

3 mentions without citation

Azoreductases in drug metabolism.
Ryan A. (2017)
2 more