X-ray diffraction
1.95Å resolution

Crystal structure of Burkholderia cenocepacia dihydropteroate synthase complexed with 7,8-dihydropteroate.


Function and Biology Details

Reaction catalysed:
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 31 KDa
Source organism: Burkholderia cenocepacia
Expression system: Escherichia coli BL21(DE3)
  • Canonical: B4E5F5 (Residues: 1-292; Coverage: 100%)
Gene names: BCAL1268, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 73.662Å b: 86.92Å c: 88.795Å
α: 90° β: 90° γ: 90°
R R work R free
0.177 0.176 0.211
Expression system: Escherichia coli BL21(DE3)