X-ray diffraction
2.5Å resolution

Function and Biology Details

Reactions catalysed:
2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-gluconate = pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 297 amino acids
Theoretical weight: 34.1 KDa
Source organism: Picrophilus torridus
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q6KZI8 (Residues: 1-266; Coverage: 100%)
Gene name: PTO1279
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Unit cell:
a: 77.954Å b: 100.159Å c: 154.609Å
α: 90° β: 90° γ: 90°
R R work R free
0.179 0.175 0.26
Expression system: Escherichia coli BL21(DE3)