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Fig. 4 | Journal of Biological Engineering

Fig. 4

From: Unique N-glycosylation of a recombinant exo-inulinase from Kluyveromyces cicerisporus and its effect on enzymatic activity and thermostability

Fig. 4

Three-dimensional structure modeling of the wild-type rKcINU1 (a) with N-glycosylation sites and (b) with N-linked glycan chains. The protein 3D model was built by the Swiss-Model server, followed by manually docking the (Man)7(GlcNAc)2 glycan chains to the Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526 residues using the program GLYCAM. The wild-type rKcINU1 folded into two domains, a N-terminal β-propeller catalytic domain (in green) and a C-terminal β-sandwich domain (in yellow) formed by two antiparallel six-stranded β-sheets, and the two domains were linked by a short loop illustrated in cyan. The N-glycosylation sites Asn-362, Asn-370, Asn-399, Asn-467 and Asn-526 and N-linked glycan chains were indicated by purple sticks and green sticks, respectively, while the catalytic active residues (Asp-30, Asp-159 and Glu-215) were shown as red sticks

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