› 1ec7

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-533002 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucarate dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 446 amino acids
Theoretical weight: 49.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AES2 (Residues: 1-446; Coverage: 100%)
Gene names: JW2758, b2787, gudD, ygcX
Sequence domains: Enolase C-terminal domain-like
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand IPA 4 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 71.25Å b: 84.55Å c: 98.92Å
α: 103.3° β: 94° γ: 113.1°
R-values:
R R work R free
0.194 not available not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
2 more

1 mention without citation

Structure of galactarate dehydratase, a new fold in an enolase involved in bacterial fitness after antibiotic treatment.
Rosas-Lemus et al. (2020)