4fl4: Difference between revisions

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-'''Unreleased structure'''
-The entry 4fl4 is ON HOLD
+==Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome==
+<StructureSection load='4fl4' size='340' side='right'caption='[[4fl4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-Authors: Currie, M.A., Adams, J.J., Faucher, F., Bayer, E.A., Jia, Z., Smith, S.P., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4fl4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p0d 3p0d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FL4 FirstGlance]. <br>
-Description: Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4fl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fl4 OCA], [https://pdbe.org/4fl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fl4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fl4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GUND_ACET2 GUND_ACET2] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
+__TOC__
+</StructureSection>
+[[Category: Acetivibrio thermocellus]]
+[[Category: Large Structures]]
+[[Category: Adams JJ]]
+[[Category: Bayer EA]]
+[[Category: Currie MA]]
+[[Category: Faucher F]]
+[[Category: Jia Z]]
+[[Category: Smith SP]]