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New page: left|200px<br /> <applet load="1dpo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dpo, resolution 1.59Å" /> '''STRUCTURE OF RAT TR...
 
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[[Image:1dpo.gif|left|200px]]<br />
<applet load="1dpo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dpo, resolution 1.59&Aring;" />
'''STRUCTURE OF RAT TRYPSIN'''<br />


==Overview==
==STRUCTURE OF RAT TRYPSIN==
The structure of a rat trypsin mutant [S195C] at a temperature of 120 K, has been refined to a crystallographic R factor of 17.4% between 12.0 and, 1.59 A and is compared with the structure of the D102N mutant at 295 K. A, reduction in the unit cell dimensions in going from room temperature to, low temperature is accompanied by a decrease in molecular surface area and, radius of gyration. The overall structure remains similar to that at room, temperature. The attainable resolution appears to be improved due to the, decrease in the fall off of intensities with resolution [reduction of the, temperature factor]. This decreases the uncertainty in the atomic, positions and allows the localization of more protein atoms and solvent, molecules in the low temperature map. The largest differences ... [[http://ispc.weizmann.ac.il/pmbin/getpm?1881877 (full description)]]
<StructureSection load='1dpo' size='340' side='right'caption='[[1dpo]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dpo]] is a 1 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=1DPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPO 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]] 1.59&#8491;</td></tr>
<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1dpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpo OCA], [https://pdbe.org/1dpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpo RCSB], [https://www.ebi.ac.uk/pdbsum/1dpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRY2_RAT TRY2_RAT]
== 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/dp/1dpo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1dpo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of a rat trypsin mutant [S195C] at a temperature of 120 K has been refined to a crystallographic R factor of 17.4% between 12.0 and 1.59 A and is compared with the structure of the D102N mutant at 295 K. A reduction in the unit cell dimensions in going from room temperature to low temperature is accompanied by a decrease in molecular surface area and radius of gyration. The overall structure remains similar to that at room temperature. The attainable resolution appears to be improved due to the decrease in the fall off of intensities with resolution [reduction of the temperature factor]. This decreases the uncertainty in the atomic positions and allows the localization of more protein atoms and solvent molecules in the low temperature map. The largest differences between the two models occur at residues with higher than average temperature factors. Several features can be localized in the solvent region of the 120 K map that are not seen in the 295 K map. These include several more water molecules as well as an interstitial sulfate ion and two interstitial benzamidine molecules.


==About this Structure==
1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures.,Earnest T, Fauman E, Craik CS, Stroud R Proteins. 1991;10(3):171-87. PMID:1881877<ref>PMID:1881877</ref>
1DPO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]] with CA, SO4 and BEN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1DPO OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures., Earnest T, Fauman E, Craik CS, Stroud R, Proteins. 1991;10(3):171-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1881877 1881877]
</div>
<div class="pdbe-citations 1dpo" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Trypsin 3D structures|Trypsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
[[Category: Single protein]]
[[Category: Stroud RM]]
[[Category: Stroud, R.M.]]
[[Category: BEN]]
[[Category: CA]]
[[Category: SO4]]
[[Category: digestion]]
[[Category: hydrolase]]
[[Category: multigene family]]
[[Category: pancreas]]
[[Category: serine protease]]
[[Category: signal]]
[[Category: zymogen]]
 
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