1e8k: Difference between revisions

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{{STRUCTURE_1e8k|  PDB=1e8k  |  SCENE=  }}
==Cyclophilin 3 Complexed With Dipeptide Ala-Pro==
===Cyclophilin 3 Complexed With Dipeptide Ala-Pro===
<StructureSection load='1e8k' size='340' side='right' caption='[[1e8k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==Function==
<table><tr><td colspan='2'>[[1e8k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8K FirstGlance]. <br>
[[http://www.uniprot.org/uniprot/CYP3_CAEEL CYP3_CAEEL]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.  
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene><br>
 
<tr><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>
==About this Structure==
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e8k RCSB], [http://www.ebi.ac.uk/pdbsum/1e8k PDBsum]</span></td></tr>
[[1e8k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8K OCA].  
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e8k_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Cyclophilin|Cyclophilin]]
*[[Cyclophilin|Cyclophilin]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:011180378</ref><references group="xtra"/><references/>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]

Revision as of 07:04, 3 October 2014

Cyclophilin 3 Complexed With Dipeptide Ala-ProCyclophilin 3 Complexed With Dipeptide Ala-Pro

Structural highlights

1e8k is a 1 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

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

See Also

1e8k, resolution 1.90Å

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