5f66: Difference between revisions
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''' | ==High-resolution isotropic multiconformer synchrotron model of CypA at 273 K== | ||
<StructureSection load='5f66' size='340' side='right' caption='[[5f66]], [[Resolution|resolution]] 1.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f66]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F66 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yuo|4yuo]]</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=5f66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f66 OCA], [http://pdbe.org/5f66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f66 RCSB], [http://www.ebi.ac.uk/pdbsum/5f66 PDBsum]</span></td></tr> | |||
[[Category: | </table> | ||
[[Category: Fraser, J | == 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. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Peptidylprolyl isomerase]] | |||
[[Category: Fraser, J S]] | |||
[[Category: Cyclophilin]] | |||
[[Category: Isomerase]] | |||
Revision as of 22:40, 30 December 2015
High-resolution isotropic multiconformer synchrotron model of CypA at 273 KHigh-resolution isotropic multiconformer synchrotron model of CypA at 273 K
Structural highlights
Function[PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
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