3tzn

X-ray diffraction
2.08Å resolution

Crystal Structure of the Yersinia pestis 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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropteroate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 30.32 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2S9PLG4 (Residues: 1-277; Coverage: 100%)
Gene names: YPO3501, dhpS, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 71.429Å b: 49.936Å c: 75.512Å
α: 90° β: 90.24° γ: 90°
R-values:
R R work R free
0.21 0.208 0.25
Expression system: Escherichia coli BL21(DE3)