3vpk: Difference between revisions
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==Crystal Structure of 6-Guanidinohexanoyl Trypsin== | |||
<StructureSection load='3vpk' size='340' side='right'caption='[[3vpk]], [[Resolution|resolution]] 1.94Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VPK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E4B:ETHYL+4-HYDROXYBENZOATE'>E4B</scene>, <scene name='pdbligand=GHS:6-CARBAMIMIDAMIDOHEXANOIC+ACID'>GHS</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vpk OCA], [https://pdbe.org/3vpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vpk RCSB], [https://www.ebi.ac.uk/pdbsum/3vpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vpk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The force driving the conversion from the acyl intermediate to the tetrahedral intermediate in the deacylation reaction of serine proteases remains unclear. The crystal structure of 6-guanidinohexanoyl trypsin was determined at pH 7.0, near the optimum reaction pH, at 1.94 A resolution. In this structure, three water molecules are observed around the catalytic site. One acts as a nucleophile to attack the acyl carbonyl carbon while the other two waters fix the position of the catalytic water through a hydrogen bond. When the acyl carbonyl oxygen oscillates thermally, the water assumes an appropriate angle to catalyze the deacylation. Proteins 2013. (c) 2012 Wiley Periodicals, Inc. | |||
Crystal structure of 6-guanidinohexanoyl trypsin near the optimum pH reveals the acyl-enzyme intermediate to be deacylated.,Masuda Y, Nitanai Y, Mizutani R, Noguchi S Proteins. 2013 Mar;81(3):526-30. doi: 10.1002/prot.24206. Epub 2012 Dec 24. PMID:23161653<ref>PMID:23161653</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vpk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin 3D structures|Trypsin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Masuda Y]] | |||
[[Category: Mizutani R]] | |||
[[Category: Nitanai Y]] | |||
[[Category: Noguchi S]] | |||
Latest revision as of 02:34, 21 November 2024
Crystal Structure of 6-Guanidinohexanoyl Trypsin
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