› 6yve

X-ray diffraction
2.1Å 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: AAA
Molecule details ›
Chain: AAA
Length: 843 amino acids
Theoretical weight: 97.42 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P00489 (Residues: 1-843; Coverage: 100%)
Gene name: PYGM
Sequence domains: Carbohydrate phosphorylase

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
2 bound ligands:
Ligand DMS 1 x DMS
Ligand PUQ 1 x PUQ
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P43212
Unit cell:
a: 126.147Å b: 126.147Å c: 115.522Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.168 0.226

Quick links

Citations

1 citations in other articles

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)