PDBe 3h2e

X-ray diffraction
2Å resolution

Structural Studies of Pterin-Based Inhibitors of Dihydropteroate Synthase


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: 297 amino acids
Theoretical weight: 32.88 KDa
Source organism: Bacillus anthracis str. A2012
Expression system: Escherichia coli
  • Canonical: Q81VW8 (Residues: 4-280; Coverage: 99%)
Gene names: GBAA_0071, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6222
Unit cell:
a: 98.063Å b: 98.063Å c: 263.945Å
α: 90° β: 90° γ: 120°
R R work R free
0.204 0.202 0.237
Expression system: Escherichia coli