3ebp

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[[Image:3ebp.png|left|200px]]
 
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{{STRUCTURE_3ebp| PDB=3ebp | SCENE= }}
{{STRUCTURE_3ebp| PDB=3ebp | SCENE= }}
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===Glycogen Phosphorylase b/flavopiridol complex===
===Glycogen Phosphorylase b/flavopiridol complex===
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{{ABSTRACT_PUBMED_23279842}}
{{ABSTRACT_PUBMED_23279842}}
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==Function==
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[[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
==About this Structure==
==About this Structure==
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==See Also==
==See Also==
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
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==Reference==
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<ref group="xtra">PMID:023279842</ref><references group="xtra"/><references/>
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Phosphorylase]]

Revision as of 12:37, 11 December 2013

Template:STRUCTURE 3ebp

Contents

Glycogen Phosphorylase b/flavopiridol complex

Template:ABSTRACT PUBMED 23279842

Function

[PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

About this Structure

3ebp is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

See Also

Reference

  • Tsitsanou KE, Hayes JM, Keramioti M, Mamais M, Oikonomakos NG, Kato A, Leonidas DD, Zographos SE. Sourcing the affinity of flavonoids for the glycogen phosphorylase inhibitor site via crystallography, kinetics and QM/MM-PBSA binding studies: Comparison of chrysin and flavopiridol. Food Chem Toxicol. 2012 Dec 29. pii: S0278-6915(12)00903-9. doi:, 10.1016/j.fct.2012.12.030. PMID:23279842 doi:http://dx.doi.org/10.1016/j.fct.2012.12.030

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