2rs4: Difference between revisions

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-==NMR strucure of stereo-array isotope labelled (SAIL) peptidyl-prolyl cis-trans isomerase from E. coli (EPPIb)==
-<StructureSection load='2rs4' size='340' side='right' caption='[[2rs4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+==NMR structure of stereo-array isotope labelled (SAIL) peptidyl-prolyl cis-trans isomerase from E. coli (EPPIb)==
+<StructureSection load='2rs4' size='340' side='right'caption='[[2rs4]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rs4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RS4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rs4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RS4 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nul|2nul]]</td></tr>
+</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=2rs4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rs4 OCA], [https://pdbe.org/2rs4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rs4 RCSB], [https://www.ebi.ac.uk/pdbsum/2rs4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rs4 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ppiB, b0525, JW0514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=2rs4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rs4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rs4 RCSB], [http://www.ebi.ac.uk/pdbsum/2rs4 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PPIB_ECOLI PPIB_ECOLI]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+[https://www.uniprot.org/uniprot/PPIB_ECOLI PPIB_ECOLI] 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 ==
@@ Line 18: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2rs4" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli k-12]]
+[[Category: Escherichia coli K-12]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Jee, J]]
+[[Category: Jee J]]
-[[Category: Kainosho, M]]
+[[Category: Kainosho M]]
-[[Category: Okuma, K]]
+[[Category: Okuma K]]
-[[Category: Ono, A M]]
+[[Category: Ono AM]]
-[[Category: Takeda, M]]
+[[Category: Takeda M]]
-[[Category: Terauchi, T]]
+[[Category: Terauchi T]]
-[[Category: Isomerase]]
-[[Category: Sail]]