9wl4: Difference between revisions

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'''Unreleased structure'''


The entry 9wl4 is ON HOLD  until Paper Publication
==Crystal structure of human glutaminyl cyclase in complex with Inhibitor CL20==
 
<StructureSection load='9wl4' size='340' side='right'caption='[[9wl4]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
Authors: Li, G.-B., Meng, F.-B.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9wl4]] is a 12 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=9WL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WL4 FirstGlance]. <br>
Description: Crystal structure of human glutaminyl cyclase in complex with Inhibitor CL20
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.436&#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=A1EXQ:3-(2,3-dimethoxyphenyl)-6-[(5-methylimidazol-1-yl)methyl]-1~{H}-pyridin-2-one'>A1EXQ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9wl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wl4 OCA], [https://pdbe.org/9wl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wl4 RCSB], [https://www.ebi.ac.uk/pdbsum/9wl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wl4 ProSAT]</span></td></tr>
[[Category: Meng, F.-B]]
</table>
== 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]]

Latest revision as of 08:06, 9 September 2026

Crystal structure of human glutaminyl cyclase in complex with Inhibitor CL20

9wl4, resolution 2.44Å

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