6u5e: Difference between revisions

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<StructureSection load='6u5e' size='340' side='right'caption='[[6u5e]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
<StructureSection load='6u5e' size='340' side='right'caption='[[6u5e]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6u5e]] 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=6U5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U5E FirstGlance]. <br>
<table><tr><td colspan='2'>[[6u5e]] 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=6U5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U5E FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#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=6u5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u5e OCA], [https://pdbe.org/6u5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u5e RCSB], [https://www.ebi.ac.uk/pdbsum/6u5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u5e 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=6u5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u5e OCA], [http://pdbe.org/6u5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u5e RCSB], [http://www.ebi.ac.uk/pdbsum/6u5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u5e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.
 
==See Also==
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Brewster AS]]
[[Category: Brewster, A S]]
[[Category: Fraser JS]]
[[Category: Fraser, J S]]
[[Category: Iwata S]]
[[Category: Iwata, S]]
[[Category: Nakane T]]
[[Category: Nakane, T]]
[[Category: Nango E]]
[[Category: Nango, E]]
[[Category: Sauter NK]]
[[Category: Sauter, N K]]
[[Category: Sugahara M]]
[[Category: Sugahara, M]]
[[Category: Tanaka R]]
[[Category: Tanaka, R]]
[[Category: Thompson MC]]
[[Category: Thompson, M C]]
[[Category: Tono K]]
[[Category: Tono, K]]
[[Category: Wolff AM]]
[[Category: Wolff, A M]]
[[Category: Young ID]]
[[Category: Young, I D]]
[[Category: Cis-tran]]
[[Category: Cyclophilin]]
[[Category: Isomerase]]
[[Category: Peptidyl-prolyl]]

Latest revision as of 10:08, 16 August 2023

RT XFEL structure of CypA solved using celloluse carrier media

6u5e, resolution 1.56Å

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