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5t3h

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==bovine trypsin soaked with selenourea for 5 min==
==bovine trypsin soaked with selenourea for 5 min==
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<StructureSection load='5t3h' size='340' side='right' caption='[[5t3h]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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<StructureSection load='5t3h' size='340' side='right'caption='[[5t3h]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t3h]] 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=5T3H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T3H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t3h]] 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=5T3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T3H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SEY:SELENOUREA'>SEY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.55&#8491;</td></tr>
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<tr id='activity'><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>
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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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SEY:SELENOUREA'>SEY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t3h OCA], [http://pdbe.org/5t3h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t3h RCSB], [http://www.ebi.ac.uk/pdbsum/5t3h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t3h ProSAT]</span></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=5t3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t3h OCA], [https://pdbe.org/5t3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t3h RCSB], [https://www.ebi.ac.uk/pdbsum/5t3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t3h ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
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Majority of novel X-ray crystal structures of proteins are currently solved using the anomalous diffraction signal provided by selenium after incorporation of selenomethionine instead of natural methionine by genetic engineering methods. However, selenium can be inserted into protein crystals in the form of selenourea (SeC(NH2)2), by adding the crystalline powder of selenourea into mother liquor or cryo-solution with native crystals, in analogy to the classic procedure of heavy-atom derivatization. Selenourea is able to bind to reactive groups at the surface of macromolecules primarily through hydrogen bonds, where the selenium atom may serve as acceptor and amide groups as donors. Selenourea has different chemical properties than heavy-atom reagents and halide ions and provides a convenient way of phasing crystal structures of macromolecules.
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Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures.,Luo Z Sci Rep. 2016 Nov 14;6:37123. doi: 10.1038/srep37123. PMID:27841370<ref>PMID:27841370</ref>
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==See Also==
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5t3h" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Trypsin]]
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[[Category: Large Structures]]
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[[Category: Dauter, Z]]
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[[Category: Dauter Z]]
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[[Category: Luo, Z]]
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[[Category: Luo Z]]
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[[Category: Hydrolase]]
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[[Category: Selenourea]]
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Current revision

bovine trypsin soaked with selenourea for 5 min

PDB ID 5t3h

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