› 1vi4

X-ray diffraction
1.87Å resolution

Function and Biology Details

Reactions catalysed: 
Oxaloacetate = pyruvate + CO(2)
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 19.55 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KPK1 (Residues: 1-161; Coverage: 100%)
Gene name: VC_2366
Sequence domains: Aldolase/RraA
Structure domains: Ribonuclease E inhibitor RraA/RraA-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: R32
Unit cell:
a: 115.33Å b: 115.33Å c: 94.585Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.282
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

3 mentions without citation

Structural and kinetic characterization of 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate degradation enzyme evolutionarily convergent with the HpaI and DmpG pyruvate aldolases.
Wang et al. (2010)
2 more