9gpb

X-ray diffraction
2.9Å resolution

THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE

Released:
Source organism: Oryctolagus cuniculus
Primary publication:
The allosteric transition of glycogen phosphorylase.
Nature 340 609-16 (1989)
PMID: 2770867

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, muscle form Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 842 amino acids
Theoretical weight: 97.29 KDa
Source organism: Oryctolagus cuniculus
Expression system: Not provided
UniProt:
  • Canonical: P00489 (Residues: 2-843; Coverage: 100%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 119Å b: 190Å c: 88.2Å
α: 90° β: 109.35° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression system: Not provided