2igw

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Current revision (10:10, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2igw' size='340' side='right'caption='[[2igw]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='2igw' size='340' side='right'caption='[[2igw]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2igw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2igw]] 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=2IGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></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]] 1.78&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2igw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igw OCA], [https://pdbe.org/2igw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igw RCSB], [https://www.ebi.ac.uk/pdbsum/2igw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igw ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2igw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igw OCA], [https://pdbe.org/2igw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igw RCSB], [https://www.ebi.ac.uk/pdbsum/2igw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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.
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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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caeel]]
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[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Kan D]]
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[[Category: Kan, D]]
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[[Category: Isomerase]]
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[[Category: Rotamase]]
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Current revision

CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PRO

PDB ID 2igw

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