5yba: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 1: Line 1:


==Dimeric Cyclophilin from T.vaginalis in complex with Myb1 peptide==
==Dimeric Cyclophilin from T.vaginalis in complex with Myb1 peptide==
<StructureSection load='5yba' size='340' side='right' caption='[[5yba]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
<StructureSection load='5yba' size='340' side='right'caption='[[5yba]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5yba]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Triva Triva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YBA FirstGlance]. <br>
<table><tr><td colspan='2'>[[5yba]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YBA FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TVAG_004440 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5722 TRIVA])</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]] 2.062&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=5yba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yba OCA], [https://pdbe.org/5yba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yba RCSB], [https://www.ebi.ac.uk/pdbsum/5yba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yba 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=5yba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yba OCA], [http://pdbe.org/5yba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yba RCSB], [http://www.ebi.ac.uk/pdbsum/5yba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yba ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A2DT06_TRIVA A2DT06_TRIVA]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019]  
[https://www.uniprot.org/uniprot/Q58HP2_TRIVA Q58HP2_TRIVA]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 23: Line 22:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Triva]]
[[Category: Trichomonas vaginalis]]
[[Category: Chen, C]]
[[Category: Chen C]]
[[Category: Cho, C C]]
[[Category: Cho CC]]
[[Category: Chou, C C]]
[[Category: Chou CC]]
[[Category: Hsu, C H]]
[[Category: Hsu CH]]
[[Category: Lin, M H]]
[[Category: Lin MH]]
[[Category: Martin, T]]
[[Category: Martin T]]
[[Category: Cyclophilin some]]
[[Category: Divergent loop cyclophilin]]
[[Category: Isomerase]]
[[Category: Rotamase complex]]