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PDBe Entry: 1c50 
IDENTIFICATION AND STRUCTURAL CHARACTERIZATION OF A NOVEL ALLOSTERIC BINDING SITE OF GLYCOGEN PHOSPHORYLASE B
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TRANSFERASE
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X-RAY DIFFRACTION
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Resolution: 2.3 Å, R-factor: 19.9%, Free R-factor: 24.6%, Spacegroup: P 43 21 2
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23/12/1999, deposition: 15/12/1999, last revision: 24/02/2009
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Oikonomakos, N.G.; Skamnaki, V.T.; Tsitsanou, K.E.; Gavalas, N.G.; Johnson, L.N.
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A new allosteric site in glycogen phosphorylase b as a target for drug interactions.
STRUCTURE vol:8, pag:575-584 (2000) [PubMed ID 10873856 ]
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GLYCOGEN METABOLISM, GLYCOGEN PHOSPHORYLASE B, INHIBITION, CENTRAL CAVITY, DRUG BINDING SITE, TRANSFERASE
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2.4.1.1 ExPASy BRENDA (A)
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Oryctolagus cuniculus(rabbit) 9986(A)
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Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase) P00489 (A)
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A
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| A |
PROTEIN (GLYCOGEN PHOSPHORYLASE) |
Protein |
P00489 (PYGM_RABIT)
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830 |
100% |
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| A |
PYRIDOXAL-5'-PHOSPHATE |
PLP
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| A |
5-CHLORO-1H-INDOLE-2-CARBOXYLIC ACID [1-(4-FLUOROBENZYL)-2-(4-HYDROXYPIPERIDIN-1YL)-2-OXOETHYL]AMIDE |
CHI
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