3nk8
From Proteopedia
(Difference between revisions)
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+ | [[Image:3nk8.jpg|left|200px]] | ||
- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3nk8", 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_3nk8| PDB=3nk8 | SCENE= }} | ||
- | + | ===Trypsin in complex with fluorine-containing fragment=== | |
- | Description: Trypsin in complex with fluorine-containing fragment | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov | + | <!-- |
+ | The line below this paragraph, {{ABSTRACT_PUBMED_20886466}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 20886466 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_20886466}} | ||
+ | |||
+ | ==About this Structure== | ||
+ | 3NK8 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NK8 OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:20886466</ref><references group="xtra"/> | ||
+ | [[Category: Bos taurus]] | ||
+ | [[Category: Trypsin]] | ||
+ | [[Category: Dalvit, C.]] | ||
+ | [[Category: Schiering, N.]] | ||
+ | [[Category: Vulpetti, A.]] | ||
+ | [[Category: Beta barrel]] | ||
+ | [[Category: Calcium binding]] | ||
+ | [[Category: Chymotrypsin double beta barrel]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Pancreas-duodenum]] | ||
+ | [[Category: Peptide hydrolase]] | ||
+ | |||
+ | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:49:54 2010'' |
Revision as of 03:38, 10 November 2010
Trypsin in complex with fluorine-containing fragment
Template:ABSTRACT PUBMED 20886466
About this Structure
3NK8 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
- Vulpetti A, Schiering N, Dalvit C. Combined use of computational chemistry, NMR screening, and X-ray crystallography for identification and characterization of fluorophilic protein environments. Proteins. 2010 Dec;78(16):3281-91. doi: 10.1002/prot.22836. PMID:20886466 doi:10.1002/prot.22836
Page seeded by OCA on Wed Nov 10 06:49:54 2010