1EM6

HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH GLCNAC AND CP-526,423

Summary for 1EM6

• Entry DOI: 10.2210/pdb1em6/pdb
• Descriptor: LIVER GLYCOGEN PHOSPHORYLASE, N-acetyl-beta-D-glucopyranosylamine, BIS[5-CHLORO-1H-INDOL-2-YL-CARBONYL-AMINOETHYL]-ETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: allosteric site, allosteric binding, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 196111.19

Authors

Rath, V.L.,Ammirati, M.,Danley, D.E.,Ekstrom, J.L.,Hynes, T.R.,Olson, T.V.,Hoover, D.J. (deposition date: 2000-03-16, release date: 2000-11-01, Last modification date: 2025-03-26)

Primary citation

Rath, V.L.,Ammirati, M.,Danley, D.E.,Ekstrom, J.L.,Gibbs, E.M.,Hynes, T.R.,Mathiowetz, A.M.,McPherson, R.K.,Olson, T.V.,Treadway, J.L.,Hoover, D.J.
Human liver glycogen phosphorylase inhibitors bind at a new allosteric site.
Chem.Biol., 7:677-682, 2000

PubMed Abstract: Glycogen phosphorylases catalyze the breakdown of glycogen to glucose-1-phosphate for glycolysis. Maintaining control of blood glucose levels is critical in minimizing the debilitating effects of diabetes, making liver glycogen phosphorylase a potential therapeutic target.

PubMed: 10980448
DOI: 10.1016/S1074-5521(00)00004-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)