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X-ray diffraction
2.2Å resolution

Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.

Released:
DOI: 10.2210/pdb1mxs/pdb
PDB entry 1mxs coloured by chain, front view.
PDB entry 1mxs coloured by chain, side view.
PDB entry 1mxs coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.
Bell BJ, Watanabe L, Rios-Steiner JL, Tulinsky A, Lebioda L, Arni RK
Acta Crystallogr D Biol Crystallogr 59 1454-8 (2003)
PMID: 12876349

Function and Biology Details

Reaction catalysed: 
2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxy-phosphogluconate aldolase Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 24 KDa
Source organism: Pseudomonas putida
UniProt:
  • Canonical: P00885 (Residues: 2-226; Coverage: 100%)
Gene name: eda
Sequence domains: KDPG and KHG aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P213
Unit cell:
a: 103.3Å b: 103.3Å c: 103.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.214

Quick links

Citations

1 review citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
3 other articles

2 mentions without citation

Key Enzymes of the Semiphosphorylative Entner-Doudoroff Pathway in the Haloarchaeon Haloferax volcanii: Characterization of Glucose Dehydrogenase, Gluconate Dehydratase, and 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase.
Sutter et al. (2016)
1 more