1dxj
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STRUCTURE OF THE CHITINASE FROM JACK BEAN
OverviewOverview
The structure of jack bean chitinase was solved at 1.8 A resolution by, molecular replacement. It is an alpha-helical protein with three disulfide, bridges. The active site is related in structure to animal and viral, lysozymes. However, unlike in lysozyme, the architecture of the active, site suggests a single-step cleavage. According to this mechanism, Glu68, is the proton donor and Glu90 assists in the reaction by moving towards, the substrate and recruiting a water molecule that acts as the, nucleophile. In this model, a water molecule was found in contact with, Glu90 O(epsilon1) and Thr119 O(gamma) at a distance of 3.0 and 2.8 A, respectively. The model is in accordance with the observed inversion, mechanism.
About this StructureAbout this Structure
1DXJ is a Single protein structure of sequence from Canavalia ensiformis with SO4 as ligand. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
ReferenceReference
Structure of jack bean chitinase., Hahn M, Hennig M, Schlesier B, Hohne W, Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1096-9. PMID:10957628
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