4fl4: Difference between revisions
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==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]] 2.80Å' scene=''> | |||
== 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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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> | ||
[[4fl4]] is a 12 chain structure with sequence from [ | <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: | [[Category: Currie MA]] | ||
[[Category: | [[Category: Faucher F]] | ||
[[Category: | [[Category: Jia Z]] | ||
[[Category: | [[Category: Smith SP]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
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Latest revision as of 14:17, 1 March 2024
Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosomeScaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome
Structural highlights
FunctionGUND_ACET2 This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
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