2y62
From Proteopedia
(Difference between revisions)
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- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_2y62", creates the "Structure Box" on the page. | ||
+ | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
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+ | {{STRUCTURE_2y62| PDB=2y62 | SCENE= }} | ||
- | + | ===CRYSTAL STRUCTURE OF LEISHMANIAL E65Q-TIM COMPLEXED WITH R-GLYCIDOL PHOSPHATE=== | |
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+ | <!-- | ||
+ | The line below this paragraph, {{ABSTRACT_PUBMED_21633986}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 21633986 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_21633986}} | ||
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+ | ==About this Structure== | ||
+ | [[2y62]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y62 OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:021633986</ref><references group="xtra"/> | ||
+ | [[Category: Leishmania mexicana]] | ||
+ | [[Category: Triose-phosphate isomerase]] | ||
+ | [[Category: Alahuhta, M.]] | ||
+ | [[Category: Pihko, P M.]] | ||
+ | [[Category: Venkatesan, R.]] | ||
+ | [[Category: Wierenga, R K.]] | ||
+ | [[Category: Enzyme-ligand complex]] | ||
+ | [[Category: Fatty acid biosynthesis]] | ||
+ | [[Category: Gluconeogenesis]] | ||
+ | [[Category: Glycolysis]] | ||
+ | [[Category: Isomerase]] | ||
+ | [[Category: Pentose shunt]] | ||
+ | [[Category: Transition state analogue]] |
Revision as of 11:39, 14 December 2011
CRYSTAL STRUCTURE OF LEISHMANIAL E65Q-TIM COMPLEXED WITH R-GLYCIDOL PHOSPHATE
Template:ABSTRACT PUBMED 21633986
About this Structure
2y62 is a 1 chain structure with sequence from Leishmania mexicana. Full crystallographic information is available from OCA.
Reference
- Venkatesan R, Alahuhta M, Pihko PM, Wierenga RK. High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active site. Protein Sci. 2011 Jun 1. doi: 10.1002/pro.667. PMID:21633986 doi:10.1002/pro.667