PDBe 3ddw

X-ray diffraction
1.9Å resolution

Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK055

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, liver form Chains: A, B
Molecule details ›
Chains: A, B
Length: 848 amino acids
Theoretical weight: 97.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06737 (Residues: 2-847; Coverage: 100%)
Gene name: PYGL
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P31
Unit cell:
a: 124.368Å b: 124.368Å c: 123.621Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.153 0.186
Expression system: Escherichia coli