5kv3: Difference between revisions

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 <StructureSection load='5kv3' size='340' side='right'caption='[[5kv3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5kv3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KV3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5kv3]] is a 1 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=5KV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KV3 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kul|5kul]], [[5kun|5kun]], [[5kuo|5kuo]], [[5kuq|5kuq]], [[5kur|5kur]], [[5kus|5kus]], [[5kuu|5kuu]], [[5kuv|5kuv]], [[5kuw|5kuw]], [[5kuz|5kuz]], [[5kv0|5kv0]], [[5kv1|5kv1]], [[5kv2|5kv2]], [[5kv4|5kv4]], [[5kv5|5kv5]], [[5kv6|5kv6]], [[5kv7|5kv7]]</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]] 1.7&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5kv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kv3 OCA], [https://pdbe.org/5kv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kv3 RCSB], [https://www.ebi.ac.uk/pdbsum/5kv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kv3 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=5kv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kv3 OCA], [http://pdbe.org/5kv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5kv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kv3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Fraser JS]]
-[[Category: Bedem, H van den]]
+[[Category: Gonzalez A]]
-[[Category: Fraser, J S]]
+[[Category: Keedy DA]]
-[[Category: Gonzalez, A]]
+[[Category: Kenner LR]]
-[[Category: Keedy, D A]]
+[[Category: Russi S]]
-[[Category: Kenner, L R]]
+[[Category: Van den Bedem H]]
-[[Category: Russi, S]]
-[[Category: Conformational variation]]
-[[Category: Isomerase]]
-[[Category: Radiation damage]]