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3ra6
From Proteopedia
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==Crystal structure of T. celer L30e E62A/K46A variant== | ==Crystal structure of T. celer L30e E62A/K46A variant== | ||
| - | <StructureSection load='3ra6' size='340' side='right' caption='[[3ra6]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3ra6' size='340' side='right'caption='[[3ra6]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ra6]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3ra6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RA6 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=3ra6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ra6 OCA], [https://pdbe.org/3ra6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ra6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ra6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ra6 ProSAT]</span></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| + | [https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding.,Chan CH, Yu TH, Wong KB PLoS One. 2011;6(6):e21624. Epub 2011 Jun 24. PMID:21720566<ref>PMID:21720566</ref> | Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding.,Chan CH, Yu TH, Wong KB PLoS One. 2011;6(6):e21624. Epub 2011 Jun 24. PMID:21720566<ref>PMID:21720566</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | <div class="pdbe-citations 3ra6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermococcus celer]] | [[Category: Thermococcus celer]] | ||
| - | [[Category: Chan | + | [[Category: Chan CH]] |
| - | [[Category: Wong | + | [[Category: Wong KB]] |
| - | [[Category: Yu | + | [[Category: Yu TH]] |
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Current revision
Crystal structure of T. celer L30e E62A/K46A variant
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