1g0c

<StructureSection load='1g0c' size='340' side='right' caption='[[1g0c]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1g0c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacs6 Bacs6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0C FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g01|1g01]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0c OCA], [http://pdbe.org/1g0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0c RCSB], [http://www.ebi.ac.uk/pdbsum/1g0c PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0c_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 A resolution. Because of the most alkaliphilic nature and it's highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.

Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme.,Shirai T, Ishida H, Noda J, Yamane T, Ozaki K, Hakamada Y, Ito S J Mol Biol. 2001 Jul 27;310(5):1079-87. PMID:11501997<ref>PMID:11501997</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1g0c" style="background-color:#fffaf0;"></div>

*[[Glucanase|Glucanase]]

[[Category: Bacs6]]

[[Category: Cellulase]]

[[Category: Hakamada, Y]]

[[Category: Ishida, H]]

[[Category: Ito, S]]

[[Category: Noda, J]]

[[Category: Ozaki, K]]

[[Category: Shirai, T]]

[[Category: Yamane, T]]

[[Category: Tim-barrel]]