› 1h6c

X-ray diffraction
2.2Å resolution

Oxidized Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis complexed with succinate

Released:
DOI: 10.2210/pdb1h6c/pdb
PDB entry 1h6c coloured by chain, front view.
PDB entry 1h6c coloured by chain, side view.
PDB entry 1h6c coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands.
Nurizzo D, Halbig D, Sprenger GA, Baker EN
Biochemistry 40 13857-67 (2001)
PMID: 11705375

Function and Biology Details

Reaction catalysed: 
D-glucose + D-fructose = D-gluconolactone + D-glucitol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
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
Molecule details ›
Chains: A, B
Length: 433 amino acids
Theoretical weight: 47.34 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07982 (Residues: 1-433; Coverage: 100%)
Gene names: ZMO0689, gfo
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand SIN 2 x SIN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 84.1Å b: 93.3Å c: 115.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.267
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein targeting by the bacterial twin-arginine translocation (Tat) pathway.
Berks et al. (2005)
2 more

1 mention without citation

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases.
Taberman et al. (2016)