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1ygp
From Proteopedia
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===PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.=== | ===PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1ygp]] is a 2 chain structure of [[Glycogen Phosphorylase]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The December 2001 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Glycogen Phosphorylase'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2001_12 10.2210/rcsb_pdb/mom_2001_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGP OCA]. | |
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| + | ==See Also== | ||
| + | *[[Glycogen Phosphorylase|Glycogen Phosphorylase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008703213</ref><references group="xtra"/> |
[[Category: Glycogen Phosphorylase]] | [[Category: Glycogen Phosphorylase]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
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[[Category: Phosphorylated form]] | [[Category: Phosphorylated form]] | ||
[[Category: Yeast]] | [[Category: Yeast]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 20 22:39:21 2010'' | ||
Revision as of 13:17, 26 July 2012
Contents |
PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.
Template:ABSTRACT PUBMED 8703213
About this Structure
1ygp is a 2 chain structure of Glycogen Phosphorylase with sequence from Saccharomyces cerevisiae. The December 2001 RCSB PDB Molecule of the Month feature on Glycogen Phosphorylase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2001_12. Full crystallographic information is available from OCA.
See Also
Reference
- Lin K, Rath VL, Dai SC, Fletterick RJ, Hwang PK. A protein phosphorylation switch at the conserved allosteric site in GP. Science. 1996 Sep 13;273(5281):1539-42. PMID:8703213
