Sequence, Structure, and Binding Analysis of Cyclodextrinase (TK1770) from T. kodakarensis (KOD1) Using an In Silico Approach

Figure 3

Structural features of Tk1770 CDase. (a) The schematic diagram representing the domain arrangement within Tk1770 made with software DOG (Domain Graph) v2.0 [32]. (b) The homology model of Tk1770 CDase consisting of N′- (blue), N- (yellow), catalytic (red), and C-domain (green). The catalytic domain also contains helix-loop-helix (HLH) structure (cyan). (c) Structural alignment of N′-domain (CBM48) of Tk1770 CDase (blue) model and template (4AEF) (grey) with an extension of loop into the catalytic site. The sequence alignment between the loops of model and template (4AEF) suggests that the substitution of P91 and S92 in Tk1770 makes its loop rigid.

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