X-ray diffraction
2.3Å resolution

Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis

Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Trehalose-6-phosphate synthase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 481 amino acids
Theoretical weight: 53.86 KDa
Source organism: Burkholderia vietnamiensis G4
Expression system: Escherichia coli
  • Canonical: A4JGS8 (Residues: 1-473; Coverage: 100%)
Gene name: Bcep1808_2483
Sequence domains: Glycosyltransferase family 20
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 96.17Å b: 103.02Å c: 218.47Å
α: 90° β: 96.42° γ: 90°
R R work R free
0.179 0.178 0.224
Expression system: Escherichia coli