4ywy
From Proteopedia
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| - | ''' | + | ==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase in complex with inhibitor PBD-150== |
| - | + | <StructureSection load='4ywy' size='340' side='right' caption='[[4ywy]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ywy]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YWY FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PBD:1-(3,4-DIMETHOXYPHENYL)-3-[3-(1H-IMIDAZOL-1-YL)PROPYL]THIOUREA'>PBD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ywy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ywy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ywy RCSB], [http://www.ebi.ac.uk/pdbsum/4ywy PDBsum]</span></td></tr> | |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[http://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: Glutaminyl-peptide cyclotransferase]] | ||
[[Category: Benvenuti, M]] | [[Category: Benvenuti, M]] | ||
| - | [[Category: Pozzi, C]] | ||
[[Category: Mangani, S]] | [[Category: Mangani, S]] | ||
| - | [[Category: | + | [[Category: Pisa, F Di]] |
| + | [[Category: Pozzi, C]] | ||
| + | [[Category: Alzheimer disease]] | ||
| + | [[Category: Cyclotransferase soluble variant]] | ||
| + | [[Category: Pbd-150 inhibitor]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 20:15, 5 August 2015
Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase in complex with inhibitor PBD-150
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