› 1ec9

X-ray diffraction
2Å resolution

E. COLI GLUCARATE DEHYDRATASE BOUND TO XYLAROHYDROXAMATE

Released:
DOI: 10.2210/pdb1ec9/pdb
PDB entry 1ec9 coloured by chain, front view.
PDB entry 1ec9 coloured by chain, side view.
PDB entry 1ec9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
Gulick AM, Hubbard BK, Gerlt JA, Rayment I
Biochemistry 39 4590-602 (2000)
PMID: 10769114

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-142489 (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

3 bound ligands:
Ligand MG 4 x MG
Ligand XYH 4 x XYH
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: 71.294Å b: 84.836Å c: 98.987Å
α: 103.14° β: 94.31° γ: 113.2°
R-values:
R R work R free
0.179 0.179 0.281
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

3 mentions without citation

A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues.
Chakraborty et al. (2012)
2 more