› 1fwr

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF KDPG ALDOLASE DOUBLE MUTANT K133Q/T161K

Released:
DOI: 10.2210/pdb1fwr/pdb
PDB entry 1fwr coloured by chain, front view.
PDB entry 1fwr coloured by chain, side view.
PDB entry 1fwr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.
Wymer N, Buchanan LV, Henderson D, Mehta N, Botting CH, Pocivavsek L, Fierke CA, Toone EJ, Naismith JH
Structure 9 1-9 (2001)
PMID: 11342129

Function and Biology Details

Reactions catalysed: 
2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
(4R)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
KHG/KDPG aldolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 213 amino acids
Theoretical weight: 22.33 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A955 (Residues: 1-213; Coverage: 100%)
Gene names: JW1839, b1850, eda, hga, kdgA
Sequence domains: KDPG and KHG aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand CIT 3 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 54.87Å b: 84.5Å c: 135.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.238 0.276
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Plasticity of enzyme active sites.
Todd et al. (2002)
10 more

1 mention without citation

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Streptococcus suis serotype 2.
Zhang et al. (2008)