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| | <StructureSection load='3zi7' size='340' side='right'caption='[[3zi7]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3zi7' size='340' side='right'caption='[[3zi7]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zi7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_thermocellum_ys Clostridium thermocellum ys]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZI7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zi7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_YS Acetivibrio thermocellus YS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZI7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zi6|3zi6]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></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=3zi7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zi7 OCA], [https://pdbe.org/3zi7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zi7 RCSB], [https://www.ebi.ac.uk/pdbsum/3zi7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zi7 ProSAT]</span></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=3zi7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zi7 OCA], [https://pdbe.org/3zi7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zi7 RCSB], [https://www.ebi.ac.uk/pdbsum/3zi7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zi7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYNY_ACETH XYNY_ACETH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Clostridium thermocellum ys]] | + | [[Category: Acetivibrio thermocellus YS]] |
| - | [[Category: Endo-1,4-beta-xylanase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bowler, M W]] | + | [[Category: Bowler MW]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
XYNY_ACETH
Publication Abstract from PubMed
Introduction: X-ray crystallography is the main tool for macromolecular structure solution at atomic resolution. It provides key information for the understanding of protein function, opening opportunities for the modulation of enzymatic mechanisms, and protein-ligand interactions. As a consequence, macromolecular crystallography plays an essential role in drug design, as well as in the a posteriori validation of drug mechanisms. Areas covered: The demand for method developments and also tools for macromolecular crystallography has significantly increased over the past 10 years. As a consequence, access to the facilities required for these investigations, such as synchrotron beamlines, became more difficult and significant efforts were dedicated to the automation of the experimental setup in laboratories. In this article, the authors describe how this was accomplished and how robot-based systems contribute to the enhancement of the macromolecular structure solution pipeline. Expert opinion: The evolution in robot technology, together with progress in X-ray beam performance and software developments, contributes to a new era in macromolecular X-ray crystallography. Highly integrated experimental environments open new possibilities for crystallography experiments. It is likely that it will also change the way this technique will be used in the future, opening the field to a larger community.
Recent progress in robot-based systems for crystallography and their contribution to drug discovery.,Ferrer JL, Larive NA, Bowler MW, Nurizzo D Expert Opin Drug Discov. 2013 May 8. PMID:23656378[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ferrer JL, Larive NA, Bowler MW, Nurizzo D. Recent progress in robot-based systems for crystallography and their contribution to drug discovery. Expert Opin Drug Discov. 2013 May 8. PMID:23656378 doi:10.1517/17460441.2013.793666
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