Structure analysis

Crystal structure of a 2-dehydro-3-deoxyphosphooctonate aldolase from Burkholderia pseudomallei in complex with D-arabinose-5-phosphate

X-ray diffraction
2.1Å resolution
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 33410.26 Å2
Buried surface area: 18892.11 Å2
Dissociation area: 3,908.09 Å2
Dissociation energy (ΔGdiss): 31.32 kcal/mol
Dissociation entropy (TΔSdiss): 15.1 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-174652

Macromolecules

Chains: A, B, C, D
Length: 285 amino acids
Theoretical weight: 30.49 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q3JP68 (Residues: 1-281; Coverage: 100%)
Gene names: BURPS1710b_3264, kdsA
Pfam: DAHP synthetase I family
InterPro:
CATH: Aldolase class I

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