3oxg
From Proteopedia
(Difference between revisions)
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- | + | [[Image:3oxg.jpg|left|200px]] | |
- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3oxg", 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), | ||
+ | or leave the SCENE parameter empty for the default display. | ||
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+ | {{STRUCTURE_3oxg| PDB=3oxg | SCENE= }} | ||
- | + | ===human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)=== | |
- | Description: human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III) | ||
- | + | <!-- | |
+ | The line below this paragraph, {{ABSTRACT_PUBMED_21266482}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 21266482 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_21266482}} | ||
+ | |||
+ | ==About this Structure== | ||
+ | [[3oxg]] is a 1 chain structure with sequence 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=3OXG OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:21266482</ref><references group="xtra"/> | ||
+ | [[Category: Histone-lysine N-methyltransferase]] | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Ding, J.]] | ||
+ | [[Category: Sun, B.]] | ||
+ | [[Category: Wu, J.]] | ||
+ | [[Category: Xu, S.]] | ||
+ | [[Category: Zhong, C.]] |
Revision as of 09:58, 23 February 2011
human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)
Template:ABSTRACT PUBMED 21266482
About this Structure
3oxg is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Xu S, Wu J, Sun B, Zhong C, Ding J. Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding. Nucleic Acids Res. 2011 Jan 25. PMID:21266482 doi:10.1093/nar/gkr019