› 2ieg

X-ray diffraction
1.9Å resolution

Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone

Released:
DOI: 10.2210/pdb2ieg/pdb
Model geometry
Fit model/data
PDB entry 2ieg coloured by chain, front view.
PDB entry 2ieg coloured by chain, side view.
PDB entry 2ieg coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors.
Birch AM, Kenny PW, Oikonomakos NG, Otterbein L, Schofield P, Whittamore PR, Whalley DP
Bioorg Med Chem Lett 17 394-9 (2007)
PMID: 17095214

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 domain:

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
Molecule details ›
Chains: A, B
Length: 842 amino acids
Theoretical weight: 97.29 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


Cofactor: Ligand PLR 2 x PLR
1 bound ligand:
Ligand FRY 2 x FRY
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 114.12Å b: 125.156Å c: 128.387Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.269

Quick links

Citations

5 review citations

Glycogen metabolism has a key role in the cancer microenvironment and provides new targets for cancer therapy.
Zois et al. (2016)
4 more

2 mentions without citation

Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers.
Harrus et al. (2018)
1 more