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1dyw

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==BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A DIVERGENT LOOP CYCLOPHILIN FROM CAENORHABDITIS ELEGANS==
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<StructureSection load='1dyw' size='340' side='right' caption='[[1dyw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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==Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans==
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<StructureSection load='1dyw' size='340' side='right'caption='[[1dyw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1dyw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DYW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1dyw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DYW FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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=1dyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyw OCA], [http://pdbe.org/1dyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dyw RCSB], [http://www.ebi.ac.uk/pdbsum/1dyw PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dyw OCA], [https://pdbe.org/1dyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dyw RCSB], [https://www.ebi.ac.uk/pdbsum/1dyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dyw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/1dyw_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/1dyw_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>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1dyw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
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*[[Cyclophilin|Cyclophilin]]
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caeel]]
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[[Category: Caenorhabditis elegans]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Dornan, J]]
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[[Category: Dornan J]]
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[[Category: Husi, H]]
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[[Category: Husi H]]
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[[Category: Page, A P]]
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[[Category: Page AP]]
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[[Category: Taylor, P]]
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[[Category: Taylor P]]
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[[Category: Walkinshaw, M D]]
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[[Category: Walkinshaw MD]]
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[[Category: Winter, A D]]
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[[Category: Winter AD]]
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[[Category: Wu, S Y]]
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[[Category: Wu SY]]
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[[Category: Isomerase]]
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[[Category: Rotamase]]
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Current revision

Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans

PDB ID 1dyw

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