1g01 | pdb_00001g01

ALKALINE CELLULASE K CATALYTIC DOMAIN

spinqualitylabelsall models 1g01, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1g01 is a 1 chain structure with sequence from Bacillus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, CD Related: 1g0c Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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