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==Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA== | ==Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA== | ||
<StructureSection load='1zkf' size='340' side='right' caption='[[1zkf]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='1zkf' size='340' side='right' caption='[[1zkf]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
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<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> | <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> | ||
<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=1zkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkf OCA], [http://pdbe.org/1zkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zkf RCSB], [http://www.ebi.ac.uk/pdbsum/1zkf 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=1zkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkf OCA], [http://pdbe.org/1zkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zkf RCSB], [http://www.ebi.ac.uk/pdbsum/1zkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zkf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zkf ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zkf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 18:36, 12 October 2017
Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNACyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA
Structural highlights
Function[PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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