› 3vcr

X-ray diffraction
1.84Å resolution

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 analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112448 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxy-phosphogluconate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 22.95 KDa
Source organism: Oleispira antarctica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D2YW47 (Residues: 1-217; Coverage: 100%)
Sequence domains: KDPG and KHG aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PYR 2 x PYR
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: R3
Unit cell:
a: 76.02Å b: 76.02Å c: 241.121Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
12 more

2 mentions without citation

Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica.
Kube et al. (2013)
1 more