› 6y55

X-ray diffraction
2.38Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132556 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen phosphorylase, muscle form Chain: A
Molecule details ›
Chain: A
Length: 843 amino acids
Theoretical weight: 97.65 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P00489 (Residues: 1-843; Coverage: 100%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase

Ligands and Environments

1 bound ligand:
Ligand O9Q 1 x O9Q
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION SUPERNOVA
Spacegroup: P43212
Unit cell:
a: 127.847Å b: 127.847Å c: 115.731Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.157 0.211

Quick links

Citations

4 citation in other articles

Identification of Novel Cathepsin B Inhibitors with Implications in Alzheimer's Disease: Computational Refining and Biochemical Evaluation.
Chitranshi et al. (2021)
3 more

1 mention without citation

An In Silico and an In Vitro Inhibition Analysis of Glycogen Phosphorylase by Flavonoids, Styrylchromones, and Pyrazoles.
Rocha et al. (2022)