5bca
From Proteopedia
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[[Category: raw-starch binding domain]] | [[Category: raw-starch binding domain]] | ||
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Revision as of 15:43, 30 October 2007
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BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES
Overview
The crystal structure of beta-amylase from Bacillus cereus var. mycoides, was determined by the multiple isomorphous replacement method. The, structure was refined to a final R-factor of 0.186 for 102,807 independent, reflections with F/sigma(F) > or = 2.0 at 2.2 A resolution with, root-mean-square deviations from ideality in bond lengths, and bond angles, of 0.014 A and 3.00 degrees, respectively. The asymmetric unit comprises, four molecules exhibiting a dimer-of-dimers structure. The enzyme, however, acts as a monomer in solution. The beta-amylase molecule folds, into three domains; the first one is the N-terminal catalytic domain with, a (beta/alpha)8 barrel, the second one is the excursion part from the, first one, and the third one is the C-terminal domain with two almost, ... [(full description)]
About this Structure
5BCA is a [Single protein] structure of sequence from [Bacillus cereus] with CA as [ligand]. Active as [Beta-amylase], with EC number [3.2.1.2]. Structure known Active Sites: CAA, CAB, CAC and CAD. Full crystallographic information is available from [OCA].
Reference
Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution., Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y, J Biochem (Tokyo). 1999 Jun;125(6):1120-30. PMID:10348915
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