2tgd: Difference between revisions
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==LACK OF THE TRANSITION STATE STABILIZATION SITE IS A FACTOR IN THE INACTIVITY OF TRYPSINOGEN, A SERINE PROTEASE ZYMOGEN. STRUCTURE OF DFP INHIBITED BOVINE TRYPSINOGEN AT 2.1 ANGSTROMS RESOLUTION== | ==LACK OF THE TRANSITION STATE STABILIZATION SITE IS A FACTOR IN THE INACTIVITY OF TRYPSINOGEN, A SERINE PROTEASE ZYMOGEN. STRUCTURE OF DFP INHIBITED BOVINE TRYPSINOGEN AT 2.1 ANGSTROMS RESOLUTION== | ||
<StructureSection load='2tgd' size='340' side='right' caption='[[2tgd]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2tgd' size='340' side='right'caption='[[2tgd]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2tgd]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2tgd]] 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=2TGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TGD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DFP:DIISOPROPYL+PHOSPHONATE'>DFP</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=DFP:DIISOPROPYL+PHOSPHONATE'>DFP</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=2tgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tgd OCA], [https://pdbe.org/2tgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tgd RCSB], [https://www.ebi.ac.uk/pdbsum/2tgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tgd ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tg/2tgd_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tg/2tgd_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 18: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Trypsin|Trypsin]] | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: Jones | [[Category: Large Structures]] | ||
[[Category: Stroud | [[Category: Jones MO]] | ||
[[Category: Stroud RM]] | |||
Latest revision as of 04:25, 21 November 2024
LACK OF THE TRANSITION STATE STABILIZATION SITE IS A FACTOR IN THE INACTIVITY OF TRYPSINOGEN, A SERINE PROTEASE ZYMOGEN. STRUCTURE OF DFP INHIBITED BOVINE TRYPSINOGEN AT 2.1 ANGSTROMS RESOLUTIONLACK OF THE TRANSITION STATE STABILIZATION SITE IS A FACTOR IN THE INACTIVITY OF TRYPSINOGEN, A SERINE PROTEASE ZYMOGEN. STRUCTURE OF DFP INHIBITED BOVINE TRYPSINOGEN AT 2.1 ANGSTROMS RESOLUTION
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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