3ceh
From Proteopedia
(Difference between revisions)
Line 23: | Line 23: | ||
==About this Structure== | ==About this Structure== | ||
- | 3CEH is a | + | 3CEH is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CEH OCA]. |
==Reference== | ==Reference== | ||
- | + | <ref group="xtra">PMID:18373353</ref><references group="xtra"/> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] | ||
- | [[Category: Single protein]] | ||
[[Category: Anderka, O.]] | [[Category: Anderka, O.]] | ||
[[Category: Defossa, E.]] | [[Category: Defossa, E.]] | ||
Line 53: | Line 52: | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:55:22 2009'' |
Revision as of 07:55, 17 February 2009
Contents |
Human liver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688
Template:ABSTRACT PUBMED 18373353
Disease
Known disease associated with this structure: Glycogen storage disease VI OMIM:[232700]
About this Structure
3CEH is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Anderka O, Loenze P, Klabunde T, Dreyer MK, Defossa E, Wendt KU, Schmoll D. Thermodynamic characterization of allosteric glycogen phosphorylase inhibitors. Biochemistry. 2008 Apr 22;47(16):4683-91. Epub 2008 Mar 29. PMID:18373353 doi:10.1021/bi702397d
Page seeded by OCA on Tue Feb 17 09:55:22 2009
Categories: Homo sapiens | Phosphorylase | Anderka, O. | Defossa, E. | Dreyer, M K. | Klabunde, T. | Loenze, P. | Schmoll, D. | Wendt, K U. | Acetylation | Allosteric enzyme | Allosteric inhibitor | Carbohydrate metabolism | Disease mutation | Glycogen metabolism | Glycogen storage disease | Glycosyltransferase | Nucleotide-binding | Phosphoprotein | Polymorphism | Protein ligand complex | Pyridoxal phosphate | Tense state | Transferase