5usw

X-ray diffraction
1.64Å resolution

The crystal structure of 7,8-dihydropteroate synthase from Vibrio fischeri ES114

Released:
Source organism: Aliivibrio fischeri ES114
Entry authors: Tan K, Zhou M, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 281 amino acids
Theoretical weight: 31.33 KDa
Source organism: Aliivibrio fischeri ES114
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5E7M1 (Residues: 1-278; Coverage: 100%)
Gene names: VF_0480, folP
Sequence domains: Pterin binding enzyme
Structure domains: Dihydropteroate synthase-like

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 91.953Å b: 65.881Å c: 94.942Å
α: 90° β: 105.83° γ: 90°
R-values:
R R work R free
0.173 0.171 0.204
Expression system: Escherichia coli BL21(DE3)