1a3h: Difference between revisions

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 <StructureSection load='1a3h' size='340' side='right'caption='[[1a3h]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1a3h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_700163 Atcc 700163]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A3H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1a3h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salipaludibacillus_agaradhaerens Salipaludibacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A3H FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></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]] 1.57&#8491;</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=1a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a3h OCA], [https://pdbe.org/1a3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a3h RCSB], [https://www.ebi.ac.uk/pdbsum/1a3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a3h ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GUN5_SALAG GUN5_SALAG]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1a3h ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The enzymatic degradation of cellulose, by cellulases, is not only industrially important in the food, paper, and textile industries but also a potentially useful method for the environmentally friendly recycling of municipal waste. An understanding of the structural and mechanistic requirements for the hydrolysis of the beta-1,4 glycosidic bonds of cellulose is an essential prerequisite for beneficial engineering of cellulases for these processes. Cellulases have been classified into 13 of the 62 glycoside hydrolase families [Henrissat, B., and Bairoch, A. (1996) Biochem J. 316, 695-696]. The structure of the catalytic core of the family 5 endoglucanase, Ce15A, from the alkalophilic Bacillus agaradherans has been solved by multiple isomorphous replacement at 1.6 A resolution. Ce15A has the (alpha/beta)8 barrel structure and signature structural features typical of the grouping of glycoside hydrolase families known as clan GH-A, with the catalytic acid/base Glu 139 and nucleophile Glu 228 on barrel strands beta 4 and beta 7 as expected. In addition to the native enzyme, the 2.0 A resolution structure of the cellobiose-bound form of the enzyme has also been determined. Cellobiose binds preferentially in the -2 and -3 subsites of the enzyme. Kinetic studies on the isolated catalytic core domain of Ce15A, using a series of reduced cellodextrins as substrates, suggest approximately five to six binding sites, consistent with the shape and size of the cleft observed by crystallography.
-Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution.,Davies GJ, Dauter M, Brzozowski AM, Bjornvad ME, Andersen KV, Schulein M Biochemistry. 1998 Feb 17;37(7):1926-32. PMID:9485319<ref>PMID:9485319</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1a3h" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Glucanase 3D structures|Glucanase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 700163]]
-[[Category: Cellulase]]
 [[Category: Large Structures]]
-[[Category: Andersen, K]]
+[[Category: Salipaludibacillus agaradhaerens]]
-[[Category: Brzozowski, A M]]
+[[Category: Andersen K]]
-[[Category: Davies, G J]]
+[[Category: Brzozowski AM]]
-[[Category: Schulein, M]]
+[[Category: Davies GJ]]
-[[Category: Cellulose degradation]]
+[[Category: Schulein M]]
-[[Category: Endoglucanase]]
-[[Category: Glycoside hydrolase family 5]]
-[[Category: Hydrolase]]