› 2gpa

X-ray diffraction
2Å resolution

ALLOSTERIC INHIBITION OF GLYCOGEN PHOSPHORYLASE A BY A POTENTIAL ANTIDIABETIC DRUG

Released:
DOI: 10.2210/pdb2gpa/pdb
PDB entry 2gpa coloured by chain, front view.
PDB entry 2gpa coloured by chain, side view.
PDB entry 2gpa coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Allosteric inhibition of glycogen phosphorylase a by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2-methyl-pyridine-3,5,6-tricarbo xylate.
Oikonomakos NG, Tsitsanou KE, Zographos SE, Skamnaki VT, Goldmann S, Bischoff H
Protein Sci 8 1930-45 (1999)
PMID: 10548038

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 Chain: A
Molecule details ›
Chain: A
Length: 842 amino acids
Theoretical weight: 97.37 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 PLP 1 x PLP
2 bound ligands:
Ligand GLC 1 x GLC
Ligand GOL 1 x GOL
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P43212
Unit cell:
a: 127.2Å b: 127.2Å c: 116.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.23

Quick links

Citations

3 review citations

Glycogen phosphorylase inhibitors for treatment of type 2 diabetes mellitus.
Treadway et al. (2001)
2 more

3 mentions without citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
2 more