PDBe 2y5j

X-ray diffraction
2.33Å resolution

Crystal structure of Burkholderia cenocepacia dihydropteroate synthase.

Released:

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

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 73.952Å b: 89.433Å c: 87.596Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.207 0.274
Expression system: Escherichia coli BL21(DE3)