PDBe 2dqw

X-ray diffraction
1.65Å resolution

Crystal Structure of Dihydropteroate Synthase (FolP) from Thermus thermophilus HB8

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Bagautdinov B, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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: 294 amino acids
Theoretical weight: 31.9 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SLV2 (Residues: 1-294; Coverage: 100%)
Gene name: TTHA0191
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: SPRING-8 BEAMLINE BL26B1
Spacegroup: P65
Unit cell:
a: 109.994Å b: 109.994Å c: 88.321Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.237
Expression system: Escherichia coli BL21(DE3)