1bh6

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spinqualitylabelsall models 1bh6, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE

Overview

The crystal structure of subtilisin DY inhibited by, N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by, molecular replacement with subtilisin Carlsberg as the starting model. The, model has been refined to a crystallographic R factor (= sigma absolute, value [(absolute value Fo) - (absolute value Fc)] / sigma (absolute value, of Fo) of 15.1% using X-ray diffraction data to 0.175 nm resolution., Subtilisin DY is an alkaline proteinase from the X-irradiated Japanese, strain DY of Bacillus licheniformis, which normally produces subtilisin, Carlsberg. It has very similar properties to subtilisin Carlsberg, with a, slightly enhanced resistance to heat and guanidine hydrochloride-induced, denaturation, in spite of the fact that the sequences of the two enzymes, differ in 31 ... [(full description)]

About this Structure

1BH6 is a [Single protein] structure of sequence from [Bacillus licheniformis] with CA, NA and 1BH as [ligands]. Active as [[1]], with EC number [3.4.21.62]. Full crystallographic information is available from [OCA].

Reference

Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg., Eschenburg S, Genov N, Peters K, Fittkau S, Stoeva S, Wilson KS, Betzel C, Eur J Biochem. 1998 Oct 15;257(2):309-18. PMID:9826175

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