1edg: Difference between revisions
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==SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C== | |||
<StructureSection load='1edg' size='340' side='right'caption='[[1edg]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1edg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum_H10 Ruminiclostridium cellulolyticum H10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDG 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]] 1.6Å</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=1edg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edg OCA], [https://pdbe.org/1edg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edg RCSB], [https://www.ebi.ac.uk/pdbsum/1edg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edg ProSAT]</span></td></tr> | |||
== | </table> | ||
[[1edg]] is a 1 chain structure | == Function == | ||
[https://www.uniprot.org/uniprot/GUNA_RUMCH GUNA_RUMCH] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1edg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1edg ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Glucanase|Glucanase]] | *[[Glucanase 3D structures|Glucanase 3D structures]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: | [[Category: Ruminiclostridium cellulolyticum H10]] | ||
[[Category: | [[Category: Czjzek M]] | ||
[[Category: Czjzek | [[Category: Ducros V]] | ||
[[Category: Ducros | [[Category: Haser R]] | ||
[[Category: Haser | |||
Latest revision as of 07:01, 7 February 2024
SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C
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