1tx7: Difference between revisions

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 ==Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)==
-<StructureSection load='1tx7' size='340' side='right' caption='[[1tx7]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='1tx7' size='340' side='right'caption='[[1tx7]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tx7]] 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=1TX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TX7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tx7]] 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=1TX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TX7 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CM:(4-CARBAMIMIDOYLPHENYL)-METHYL-PHOSPHINIC+ACID'>4CM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><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]] 1.75&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CM:(4-CARBAMIMIDOYLPHENYL)-METHYL-PHOSPHINIC+ACID'>4CM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tx7 RCSB], [http://www.ebi.ac.uk/pdbsum/1tx7 PDBsum]</span></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=1tx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx7 OCA], [https://pdbe.org/1tx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tx7 RCSB], [https://www.ebi.ac.uk/pdbsum/1tx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx7 ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1tx7_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1tx7_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tx7 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-p-amidinophenylmethylphosphinic acid (AMPA) was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site. In comparison to benzamidine, AMPA shows improved activity, which the crystal structure demonstrates to result from hydrogen bonds between the negatively charged phosphinic acid group and the catalytic residues at the oxyanion hole.
-An oxyanion-hole selective serine protease inhibitor in complex with trypsin.,Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:11738605<ref>PMID:11738605</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Trypsin|Trypsin]]
+*[[Trypsin 3D structures|Trypsin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Trypsin]]
+[[Category: Large Structures]]
-[[Category: Crich, D.]]
+[[Category: Crich D]]
-[[Category: Cui, J.]]
+[[Category: Cui J]]
-[[Category: Fu, W.]]
+[[Category: Fu W]]
-[[Category: Johnson, M E.]]
+[[Category: Johnson ME]]
-[[Category: Marankan, F.]]
+[[Category: Marankan F]]
-[[Category: Mesecar, A.]]
+[[Category: Mesecar A]]
-[[Category: Bovine]]
-[[Category: Hydrolase]]
-[[Category: Trypsin]]