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8hy3

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'''Unreleased structure'''
 
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The entry 8hy3 is ON HOLD until Paper Publication
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==Crystal structure of human secretory glutaminyl cyclase in complex with 1-benzyl-5-methyl-1H-imidazole==
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<StructureSection load='8hy3' size='340' side='right'caption='[[8hy3]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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Authors: Li, G.-B., Deng, J.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8hy3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HY3 FirstGlance]. <br>
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Description: Crystal structure of human secretory glutaminyl cyclase in complex with 1-benzyl-5-methyl-1H-imidazole
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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]] 1.952&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4Q8:5-methyl-1-(phenylmethyl)imidazole'>4Q8</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Li, G.-B]]
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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=8hy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hy3 OCA], [https://pdbe.org/8hy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hy3 RCSB], [https://www.ebi.ac.uk/pdbsum/8hy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hy3 ProSAT]</span></td></tr>
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[[Category: Deng, J]]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Deng J]]
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[[Category: Li G-B]]

Current revision

Crystal structure of human secretory glutaminyl cyclase in complex with 1-benzyl-5-methyl-1H-imidazole

PDB ID 8hy3

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