› 3e3l

X-ray diffraction
2.59Å resolution

The R-state Glycogen Phosphorylase

Released:
DOI: 10.2210/pdb3e3l/pdb
PDB entry 3e3l coloured by chain, front view.
PDB entry 3e3l coloured by chain, side view.
PDB entry 3e3l coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Glycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators.
Leonidas DD, Zographos SE, Tsitsanou KE, Skamnaki VT, Stravodimos G, Kyriakis E
Acta Crystallogr F Struct Biol Commun 77 303-311 (2021)
PMID: 34473107

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 842 amino acids
Theoretical weight: 97.52 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P00489 (Residues: 2-843; Coverage: 100%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P21
Unit cell:
a: 118.895Å b: 189.92Å c: 88.16Å
α: 90° β: 109.27° γ: 90°
R-values:
R R work R free
0.21 0.207 0.266

Quick links

Citations

3 citation in other articles

Allosteric Regulation of Glycogen Phosphorylase by Order/Disorder Transition of the 250' and 280s Loops.
Kish et al. (2023)
2 more

1 mention without citation

Glycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators.
Leonidas et al. (2021)