1e5t

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Current revision (11:53, 13 December 2023) (edit) (undo)
 
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<StructureSection load='1e5t' size='340' side='right'caption='[[1e5t]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1e5t' size='340' side='right'caption='[[1e5t]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1e5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1e5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5T 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=GOL:GLYCEROL'>GOL</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]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qfm|1qfm]], [[1qfs|1qfs]]</div></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=GOL:GLYCEROL'>GOL</scene></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/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1e5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5t OCA], [https://pdbe.org/1e5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5t RCSB], [https://www.ebi.ac.uk/pdbsum/1e5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5t 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=1e5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5t OCA], [https://pdbe.org/1e5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5t RCSB], [https://www.ebi.ac.uk/pdbsum/1e5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG]] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
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[https://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pig]]
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[[Category: Sus scrofa]]
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[[Category: Prolyl oligopeptidase]]
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[[Category: Fulop V]]
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[[Category: Fulop, V]]
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[[Category: Alpha/ beta-hydrolase]]
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[[Category: Amnesia]]
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[[Category: Beta-propeller]]
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[[Category: Hydrolase]]
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Current revision

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

PDB ID 1e5t

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