3uvt: Difference between revisions

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OCA

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 ==Crystal structure of the third catalytic domain of ERp46==
-<StructureSection load='3uvt' size='340' side='right' caption='[[3uvt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3uvt' size='340' side='right'caption='[[3uvt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3uvt]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UVT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3uvt]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TXNDC5, TLP46, UNQ364/PRO700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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 id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=3uvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvt OCA], [https://pdbe.org/3uvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvt RCSB], [https://www.ebi.ac.uk/pdbsum/3uvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvt ProSAT]</span></td></tr>
-<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=3uvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uvt RCSB], [http://www.ebi.ac.uk/pdbsum/3uvt PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TXND5_HUMAN TXND5_HUMAN]] Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity).
+[https://www.uniprot.org/uniprot/TXND5_HUMAN TXND5_HUMAN] Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide-isomerase deficiency in yeast (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3uvt" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 27: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein disulfide-isomerase]]
+[[Category: Large Structures]]
-[[Category: Gehring, K]]
+[[Category: Gehring K]]
-[[Category: Gulerez, I E]]
+[[Category: Gulerez IE]]
-[[Category: Kozlov, G]]
+[[Category: Kozlov G]]
-[[Category: Isomerase]]
-[[Category: Thioredoxin-like fold]]