› 2g8s

X-ray diffraction
1.5Å resolution

Crystal structure of the soluble Aldose sugar dehydrogenase (Asd) from Escherichia coli in the apo-form

Released:
DOI: 10.2210/pdb2g8s/pdb
PDB entry 2g8s coloured by chain, front view.
PDB entry 2g8s coloured by chain, side view.
PDB entry 2g8s coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity.
Southall SM, Doel JJ, Richardson DJ, Oubrie A
J Biol Chem 281 30650-9 (2006)
PMID: 16864586

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-550513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldose sugar dehydrogenase YliI Chains: A, B
Molecule details ›
Chains: A, B
Length: 353 amino acids
Theoretical weight: 39.25 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P75804 (Residues: 21-370; Coverage: 100%)
Gene names: JW0821, b0837, yliI
Sequence domains: Glucose / Sorbosone dehydrogenase
Structure domains: TolB, C-terminal domain

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand PO4 1 x PO4
Ligand EDO 25 x EDO
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 40.829Å b: 113.475Å c: 75.372Å
α: 90° β: 90.03° γ: 90°
R-values:
R R work R free
0.149 0.149 0.183
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Review of glucose oxidases and glucose dehydrogenases: a bird's eye view of glucose sensing enzymes.
Ferri et al. (2011)
18 other articles

5 mentions without citation

Discovery of a eukaryotic pyrroloquinoline quinone-dependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes.
Matsumura et al. (2014)
4 more