1edg

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[[Image:1edg.png|left|200px]]
 
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{{STRUCTURE_1edg| PDB=1edg | SCENE= }}
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==SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C==
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<StructureSection load='1edg' size='340' side='right'caption='[[1edg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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===SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C===
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== Structural highlights ==
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<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>
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{{ABSTRACT_PUBMED_8535787}}
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<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>
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==About this Structure==
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</table>
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[[1edg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDG OCA].
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1edg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Glucanase|Glucanase]]
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:008535787</ref><references group="xtra"/>
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[[Category: Large Structures]]
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[[Category: Cellulase]]
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[[Category: Ruminiclostridium cellulolyticum H10]]
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[[Category: Clostridium cellulolyticum]]
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[[Category: Czjzek M]]
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[[Category: Czjzek, M.]]
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[[Category: Ducros V]]
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[[Category: Ducros, V.]]
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[[Category: Haser R]]
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[[Category: Haser, R.]]
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[[Category: Cellulase]]
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[[Category: Cellulose degradation]]
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[[Category: Family 5 of glycosyl hydrolase]]
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[[Category: Family some]]
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[[Category: Xylanase]]
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Current revision

SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C

PDB ID 1edg

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