› 3cop

X-ray diffraction
2.3Å resolution

Crystal Structure of E.coli GS mutant E377A in complex with ADP and acceptor analogue HEPPSO

Released:
DOI: 10.2210/pdb3cop/pdb
PDB entry 3cop coloured by chain, front view.
PDB entry 3cop coloured by chain, side view.
PDB entry 3cop coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.
Sheng F, Jia X, Yep A, Preiss J, Geiger JH
J Biol Chem 284 17796-807 (2009)
PMID: 19244233

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen synthase Chain: A
Molecule details ›
Chain: A
Length: 485 amino acids
Theoretical weight: 53.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6U8 (Residues: 1-477; Coverage: 100%)
Gene names: JW3392, b3429, glgA
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

3 bound ligands:
Ligand GLC 1 x GLC
Ligand ADP 1 x ADP
Ligand 250 1 x 250
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I41
Unit cell:
a: 125.84Å b: 125.84Å c: 151.958Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.197
Expression system: Escherichia coli

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Citations

7 review citations

Glycogen and its metabolism: some new developments and old themes.
Roach et al. (2012)
6 more