› 2bzs

X-ray diffraction
2Å resolution

Binding of anti-cancer prodrug CB1954 to the activating enzyme NQO2 revealed by the crystal structure of their complex.

Released:
DOI: 10.2210/pdb2bzs/pdb
PDB entry 2bzs coloured by chain, front view.
PDB entry 2bzs coloured by chain, side view.
PDB entry 2bzs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of the anticancer prodrug CB1954 to the activating enzyme NQO2 revealed by the crystal structure of their complex.
AbuKhader M, Heap J, De Matteis C, Kellam B, Doughty SW, Minton N, Paoli M
J Med Chem 48 7714-9 (2005)
PMID: 16302811

Function and Biology Details

Reaction catalysed: 
1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a quinol
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-147595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosyldihydronicotinamide dehydrogenase [quinone] Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 26.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16083 (Residues: 2-231; Coverage: 100%)
Gene names: NMOR2, NQO2
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand ZN 2 x ZN
Ligand CB1 2 x CB1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 80.83Å b: 106.11Å c: 61.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.247
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

The target landscape of clinical kinase drugs.
Klaeger et al. (2017)