› 3sz8

X-ray diffraction
2.05Å resolution

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxyphosphooctonate aldolase Chains: A, B, C, D
Molecule details ›
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
Sequence domains: DAHP synthetase I family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 85.49Å b: 83.32Å c: 87.87Å
α: 90° β: 116.59° γ: 90°
R-values:
R R work R free
0.185 0.183 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

1 mention without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)