› 1qbi

X-ray diffraction
1.72Å resolution

SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS

Released:
DOI: 10.2210/pdb1qbi/pdb
PDB entry 1qbi coloured by chain, front view.
PDB entry 1qbi coloured by chain, side view.
PDB entry 1qbi coloured by chain, top view.
Source organism: Acinetobacter calcoaceticus
Primary publication:
The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat.
Oubrie A, Rozeboom HJ, Kalk KH, Duine JA, Dijkstra BW
J Mol Biol 289 319-33 (1999)
PMID: 10366508

Function and Biology Details

Reaction catalysed: 
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146684 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Quinoprotein glucose dehydrogenase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 454 amino acids
Theoretical weight: 50.29 KDa
Source organism: Acinetobacter calcoaceticus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13650 (Residues: 25-478; Coverage: 100%)
Gene name: gdhB
Sequence domains: Glucose / Sorbosone dehydrogenase
Structure domains: TolB, C-terminal domain

Ligands and Environments

3 bound ligands:
Ligand PT 2 x PT
Ligand CA 6 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 60.148Å b: 92.1Å c: 84.91Å
α: 90° β: 105.17° γ: 90°
R-values:
R R work R free
0.166 0.165 0.208
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Beta propellers: structural rigidity and functional diversity.
Fülöp et al. (1999)
5 more

5 mentions without citation

Determination of enzyme mechanisms by molecular dynamics: studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenase.
Reddy et al. (2004)
4 more