2afx
From Proteopedia
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- | [[Image:2afx.png|left|200px]] | ||
- | + | ==Crystal structure of human glutaminyl cyclase in complex with 1-benzylimidazole== | |
+ | <StructureSection load='2afx' size='340' side='right'caption='[[2afx]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2afx]] is a 2 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=2AFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AFX FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1BN:1-BENZYL-1H-IMIDAZOLE'>1BN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2afx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afx OCA], [https://pdbe.org/2afx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2afx RCSB], [https://www.ebi.ac.uk/pdbsum/2afx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2afx ProSAT]</span></td></tr> | ||
+ | </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> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/2afx_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2afx ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Glutaminyl cyclase|Glutaminyl cyclase]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | [[ | + | </StructureSection> |
- | + | ||
- | == | + | |
- | < | + | |
- | + | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Cheng WJ]] |
- | [[Category: | + | [[Category: Huang KF]] |
- | [[Category: | + | [[Category: Ko TP]] |
- | [[Category: | + | [[Category: Liu YL]] |
- | [[Category: | + | [[Category: Wang AHJ]] |
- | + | ||
- | + |
Current revision
Crystal structure of human glutaminyl cyclase in complex with 1-benzylimidazole
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Categories: Homo sapiens | Large Structures | Cheng WJ | Huang KF | Ko TP | Liu YL | Wang AHJ