X-ray diffraction
1.92Å resolution

Structure of Mycobacterium thermoresistibile trehalose-6-phosphate synthase in a complex with Trehalose-6-phosphate.


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha,alpha-trehalose-phosphate synthase (ADP-forming) Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 54.68 KDa
Source organism: Mycolicibacterium thermoresistibile
Expression system: Escherichia coli BL21(DE3)
  • Canonical: G7CGT2 (Residues: 1-486; Coverage: 100%)
Gene name: KEK_14123
Sequence domains: Glycosyltransferase family 20
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, G6P
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: I4122
Unit cell:
a: 127.225Å b: 127.225Å c: 207.605Å
α: 90° β: 90° γ: 90°
R R work R free
0.15 0.149 0.174
Expression system: Escherichia coli BL21(DE3)