› 1ofg

X-ray diffraction
2.7Å resolution

GLUCOSE-FRUCTOSE OXIDOREDUCTASE

Released:
DOI: 10.2210/pdb1ofg/pdb
PDB entry 1ofg coloured by chain, front view.
PDB entry 1ofg coloured by chain, side view.
PDB entry 1ofg coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Kingston RL, Scopes RK, Baker EN
Structure 4 1413-28 (1996)
PMID: 8994968

Function and Biology Details

Reaction catalysed: 
D-glucose + D-fructose = D-gluconolactone + D-glucitol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose--fructose oxidoreductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 381 amino acids
Theoretical weight: 42.21 KDa
Source organism: Zymomonas mobilis
UniProt:
  • Canonical: Q07982 (Residues: 53-433; Coverage: 100%)
Gene names: ZMO0689, gfo
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 6 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 84.49Å b: 283.69Å c: 116.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 not available

Quick links

Citations

3 review citations

The Tat protein export pathway.
Berks et al. (2000)
2 more

5 mentions without citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
4 more