PDBe 3o3c

X-ray diffraction
3.51Å resolution

Glycogen synthase basal state UDP complex

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis for glucose-6-phosphate activation of glycogen synthase.
Proc. Natl. Acad. Sci. U.S.A. 107 17563-8 (2010)
PMID: 20876143

Function and Biology Details

Reaction catalysed:
UDP-alpha-D-glucose + ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha- D-glucosyl)(n+1). 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen [starch] synthase isoform 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 725 amino acids
Theoretical weight: 82.11 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P27472 (Residues: 1-705; Coverage: 100%)
Gene names: GSY2, L8479.8, YLR258W
Sequence domains: Glycogen synthase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 96.586Å b: 167.209Å c: 121.251Å
α: 90° β: 102.66° γ: 90°
R-values:
R R work R free
0.221 0.219 0.249
Expression system: Escherichia coli BL21