› 2oqy

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
Galactarate = (2S,3R)-2,3-dihydroxy-5-oxohexanedioate + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184426 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactarate dehydratase (D-threo-forming) Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 391 amino acids
Theoretical weight: 44.4 KDa
Source organism: Oceanobacillus iheyensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EMJ9 (Residues: 1-391; Coverage: 100%)
Gene name: OB2843
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 16 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 104.635Å b: 104.64Å c: 104.462Å
α: 109.5° β: 109.45° γ: 109.47°
R-values:
R R work R free
0.215 0.215 0.229
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The Enzyme Function Initiative.
Gerlt et al. (2011)
1 more

4 mentions without citation

Divergent evolution in enolase superfamily: strategies for assigning functions.
Gerlt et al. (2012)
3 more