4n1q
From Proteopedia
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==Structure of Cyclophilin A in complex with cyclohexanecarboxamide.== | ==Structure of Cyclophilin A in complex with cyclohexanecarboxamide.== | ||
<StructureSection load='4n1q' size='340' side='right' caption='[[4n1q]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='4n1q' size='340' side='right' caption='[[4n1q]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1m|4n1m]], [[4n1n|4n1n]], [[4n1o|4n1o]], [[4n1p|4n1p]], [[4n1r|4n1r]], [[4n1s|4n1s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1m|4n1m]], [[4n1n|4n1n]], [[4n1o|4n1o]], [[4n1p|4n1p]], [[4n1r|4n1r]], [[4n1s|4n1s]]</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='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=4n1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n1q RCSB], [http://www.ebi.ac.uk/pdbsum/4n1q PDBsum]</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=4n1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1q OCA], [http://pdbe.org/4n1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n1q RCSB], [http://www.ebi.ac.uk/pdbsum/4n1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1q 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. | [[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. | ||
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| + | ==See Also== | ||
| + | *[[Cyclophilin|Cyclophilin]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:04, 17 May 2017
Structure of Cyclophilin A in complex with cyclohexanecarboxamide.
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