PDBe 3tr9

X-ray diffraction
1.9Å resolution

Structure of a dihydropteroate synthase (folP) in complex with pteroic acid from Coxiella burnetii

Released:

Function and Biology Details

Reaction catalysed:
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer
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: 314 amino acids
Theoretical weight: 35.88 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83BY6 (Residues: 1-297; Coverage: 100%)
Gene names: CBU_1351, 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: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 86.877Å b: 86.883Å c: 158.159Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.212
Expression system: Escherichia coli BL21(DE3)