6tsh

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m (Protected "6tsh" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6tsh is ON HOLD
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==Beta-galactosidase in complex with deoxygalacto-nojirimycin==
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<StructureSection load='6tsh' size='340' side='right'caption='[[6tsh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6tsh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TSH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TSH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGJ:(2R,3S,4R,5S)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>DGJ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>
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<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=6tsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tsh OCA], [http://pdbe.org/6tsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tsh RCSB], [http://www.ebi.ac.uk/pdbsum/6tsh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tsh ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recent advances in cryo-electron microscopy (EM) structure determination have pushed the resolutions obtainable by the method into the range widely considered to be of utility for drug discovery. Here, we review the use of cryo-EM in fragment-based drug discovery (FBDD) based on in-house method development. We demonstrate not only that cryo-EM can reveal details of the molecular interactions between fragments and a protein, but also that the current reproducibility, quality, and throughput are compatible with FBDD. We exemplify this using the test system beta-galactosidase (Bgal) and the oncology target pyruvate kinase 2 (PKM2).
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Authors:
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Fragment-based drug discovery using cryo-EM.,Saur M, Hartshorn MJ, Dong J, Reeks J, Bunkoczi G, Jhoti H, Williams PA Drug Discov Today. 2019 Dec 23. pii: S1359-6446(19)30465-9. doi:, 10.1016/j.drudis.2019.12.006. PMID:31877353<ref>PMID:31877353</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6tsh" style="background-color:#fffaf0;"></div>
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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: Beta-galactosidase]]
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[[Category: Large Structures]]
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[[Category: Bunkoczi, G]]
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[[Category: Dong, J]]
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[[Category: Hartshorn, M J]]
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[[Category: Jhoti, H]]
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[[Category: Reeks, J]]
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[[Category: Saur, M]]
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[[Category: Williams, P A]]
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[[Category: Bgal]]
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[[Category: Nojirimycin]]
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[[Category: Sugar binding protein]]

Revision as of 07:41, 8 January 2020

Beta-galactosidase in complex with deoxygalacto-nojirimycin

PDB ID 6tsh

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