2cqb: Difference between revisions

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==Solution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase E==
==Solution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase E==
<StructureSection load='2cqb' size='340' side='right' caption='[[2cqb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2cqb' size='340' side='right' caption='[[2cqb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIE ([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=2cqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cqb OCA], [http://pdbe.org/2cqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cqb RCSB], [http://www.ebi.ac.uk/pdbsum/2cqb PDBsum], [http://www.topsan.org/Proteins/RSGI/2cqb TOPSAN]</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=2cqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cqb OCA], [http://pdbe.org/2cqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cqb RCSB], [http://www.ebi.ac.uk/pdbsum/2cqb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cqb ProSAT], [http://www.topsan.org/Proteins/RSGI/2cqb TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/2cqb_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/2cqb_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata 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=2cqb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>



Revision as of 11:19, 23 May 2018

Solution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase ESolution Structure of the RNA recognition motif in Peptidyl-prolyl cis-trans isomerase E

Structural highlights

2cqb is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:PPIE (HUMAN)
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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