3ra5: Difference between revisions

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 ==Crystal structure of T. celer L30e E6A/R92A variant==
-<StructureSection load='3ra5' size='340' side='right' caption='[[3ra5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='3ra5' size='340' side='right'caption='[[3ra5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ra5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RA5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ra5]] is a 2 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=3RA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RA5 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h7m|1h7m]], [[3ra6|3ra6]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpl30, rpl30e ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2264 Thermococcus celer])</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=3ra5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ra5 OCA], [https://pdbe.org/3ra5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ra5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ra5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ra5 ProSAT]</span></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=3ra5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ra5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ra5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ra5 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 16: @@
 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 MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3ra5" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermococcus celer]]
-[[Category: Chan, C H.]]
+[[Category: Chan CH]]
-[[Category: Wong, K B.]]
+[[Category: Wong KB]]
-[[Category: Globular protein]]
-[[Category: L30e]]
-[[Category: Ribosomal protein]]
-[[Category: Thermophilic]]