› 1dxf

X-ray diffraction
2.6Å resolution

2-dehydro-3-deoxy-galactarate aldolase from Escherichia coli in complex with pyruvate

Released:
DOI: 10.2210/pdb1dxf/pdb
PDB entry 1dxf coloured by chain, front view.
PDB entry 1dxf coloured by chain, side view.
PDB entry 1dxf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism.
Izard T, Blackwell NC
EMBO J 19 3849-56 (2000)
PMID: 10921867

Function and Biology Details

Reaction catalysed: 
2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149992 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-keto-4-deoxy-D-glucarate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 256 amino acids
Theoretical weight: 27.5 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P23522 (Residues: 1-256; Coverage: 100%)
Gene names: JW3095, b3126, garL, yhaF
Sequence domains: HpcH/HpaI aldolase/citrate lyase family
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:
Ligand PYR 2 x PYR
Ligand MG 2 x MG
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: R32
Unit cell:
a: 126.4Å b: 126.4Å c: 172Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.173 0.233

Quick links

Citations

3 review citations

Intramolecular cyclizations of polyketide biosynthesis: mining for a "Diels-Alderase"?
Kelly WL. (2008)
2 more

3 mentions without citation

Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism.
Izard et al. (2000)
2 more