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1trm

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(New page: 200px<br /><applet load="1trm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1trm, resolution 2.3&Aring;" /> '''THE THREE-DIMENSIONAL...)
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[[Image:1trm.gif|left|200px]]<br /><applet load="1trm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1trm, resolution 2.3&Aring;" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS==
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The structure of the Asn102 mutant of trypsin was determined in order to, distinguish whether the reduced activity of the mutant at neutral pH, results from an altered active site conformation or from an inability to, stabilize a positive charge on the active site histidine. The active site, structure of the Asn102 mutant of trypsin is identical to the native, enzyme with respect to the specificity pocket, the oxyanion hole, and the, orientation of the nucleophilic serine. The observed decrease in rate, results from the loss of nucleophilicity of the active site serine. This, decreased nucleophilicity may result from stabilization of a His57, tautomer that is unable to accept the serine hydroxyl proton.
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<StructureSection load='1trm' size='340' side='right'caption='[[1trm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1trm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TRM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1trm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1trm OCA], [https://pdbe.org/1trm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1trm RCSB], [https://www.ebi.ac.uk/pdbsum/1trm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1trm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRY2_RAT TRY2_RAT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tr/1trm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1trm ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TRM OCA].
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis., Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS, Science. 1987 Aug 21;237(4817):905-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3112942 3112942]
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Rattus rattus]]
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[[Category: Single protein]]
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[[Category: Fletterick RJ]]
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[[Category: Trypsin]]
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[[Category: Sprang S]]
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[[Category: Fletterick, R.J.]]
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[[Category: Standing T]]
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[[Category: Sprang, S.]]
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[[Category: Standing, T.]]
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[[Category: BEN]]
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[[Category: CA]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:32:31 2007''
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Current revision

THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS

PDB ID 1trm

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