X-ray diffraction
2.5Å resolution

Crystal structure of trehalose synthase TreT mutant E326A from P. horishiki in complex with UDP


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Trehalose synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 416 amino acids
Theoretical weight: 48.18 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
  • Canonical: O58762 (Residues: 2-415; Coverage: 100%)
Gene names: PH1035, treT
Sequence domains: Glycosyl transferases group 1
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P21
Unit cell:
a: 80.874Å b: 63.017Å c: 91.107Å
α: 90° β: 98.84° γ: 90°
R R work R free
0.209 0.209 0.271
Expression system: Escherichia coli