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4Z5X

Glycogen phosphorylase in complex with gallic acid

Summary for 4Z5X
Entry DOI10.2210/pdb4z5x/pdb
Related4YUA
DescriptorGlycogen phosphorylase, muscle form, 3,4,5-trihydroxybenzoic acid, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
Functional Keywordsalpha and beta protein, transferase
Biological sourceOryctolagus cuniculus (Rabbit)
Total number of polymer chains1
Total formula weight97855.66
Authors
Kyriakis, E.,Kantsadi, L.A.,Stravodimos, A.G.,Chatzileontiadou, S.M.D.,Leonidas, D.D. (deposition date: 2015-04-03, release date: 2015-05-13, Last modification date: 2025-04-09)
Primary citationKyriakis, E.,Stravodimos, G.A.,Kantsadi, A.L.,Chatzileontiadou, D.S.,Skamnaki, V.T.,Leonidas, D.D.
Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b.
Febs Lett., 589:1787-1794, 2015
Cited by
PubMed Abstract: We present a study on the binding of gallic acid and its dimer ellagic acid to glycogen phosphorylase (GP). Ellagic acid is a potent inhibitor with Kis of 13.4 and 7.5 μM, in contrast to gallic acid which displays Kis of 1.7 and 3.9 mM for GPb and GPa, respectively. Both compounds are competitive inhibitors with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. However, only ellagic acid functions with glucose in a strongly synergistic mode. The crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes were determined at high resolution, revealing that both ligands bind to the inhibitor binding site of the enzyme and highlight the structural basis for the significant difference in their inhibitory potency.
PubMed: 25980608
DOI: 10.1016/j.febslet.2015.05.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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