9lzv: Difference between revisions

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'''Unreleased structure'''


The entry 9lzv is ON HOLD  until Paper Publication
==Crystal structure of human glutaminyl cyclase in complex with Inhibitor M-42==
 
<StructureSection load='9lzv' size='340' side='right'caption='[[9lzv]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
Authors: Li, G.-B., Meng, F.-B., Mou, J.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9lzv]] is a 6 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=9LZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LZV FirstGlance]. <br>
Description: Crystal structure of human glutaminyl cyclase in complex with Inhibitor M-42
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1EMG:3-(1~{H}-benzimidazol-5-yl)-5-[1-[2-(3,4-dimethoxyphenyl)ethanoyl]piperidin-4-yl]oxy-1~{H}-benzimidazol-2-one'>A1EMG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Li, G.-B]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9lzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lzv OCA], [https://pdbe.org/9lzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lzv RCSB], [https://www.ebi.ac.uk/pdbsum/9lzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lzv ProSAT]</span></td></tr>
[[Category: Meng, F.-B]]
</table>
[[Category: Mou, J]]
== Function ==
[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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Li G-B]]
[[Category: Meng F-B]]
[[Category: Mou J]]

Latest revision as of 07:46, 4 March 2026

Crystal structure of human glutaminyl cyclase in complex with Inhibitor M-42

9lzv, resolution 2.33Å

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