3sre
From Proteopedia
(Difference between revisions)
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- | + | [[Image:3sre.jpg|left|200px]] | |
- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3sre", creates the "Structure Box" on the page. | ||
+ | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
+ | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
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+ | {{STRUCTURE_3sre| PDB=3sre | SCENE= }} | ||
- | + | ===Serum paraoxonase-1 by directed evolution at pH 6.5=== | |
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+ | <!-- | ||
+ | The line below this paragraph, {{ABSTRACT_PUBMED_22387469}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 22387469 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_22387469}} | ||
+ | |||
+ | ==About this Structure== | ||
+ | [[3sre]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SRE OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:022387469</ref><references group="xtra"/> | ||
+ | [[Category: Arylesterase]] | ||
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: David, M Ben.]] | ||
+ | [[Category: Elias, M.]] | ||
+ | [[Category: Silman, I.]] | ||
+ | [[Category: Sussman, J L.]] | ||
+ | [[Category: Tawfik, D S.]] | ||
+ | [[Category: 6-blades-propeller fold]] | ||
+ | [[Category: Directed evolution]] | ||
+ | [[Category: Hydrolase]] |
Revision as of 07:31, 21 March 2012
Serum paraoxonase-1 by directed evolution at pH 6.5
Template:ABSTRACT PUBMED 22387469
About this Structure
3sre is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA.
Reference
- Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS. Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1. J Mol Biol. 2012 Mar 1. PMID:22387469 doi:10.1016/j.jmb.2012.02.042