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Fig. 1 | Biotechnology for Biofuels and Bioproducts

Fig. 1

From: Structural insights into curdlan degradation via a glycoside hydrolase containing a disruptive carbohydrate-binding module

Fig. 1

Overall structure of CBM6E. a Domain architecture of CBM6E. The CBM6E protein contains a tandem arrangement of two domains: GH128 and CBM6. SP, signal peptide. b Overall structure of the tandem GH128 and CBM6 domain of CBM6E. The catalytic GH128 module adopts an (α/β) barrel scaffold, where the α-helices are depicted in magenta and the β-sheet in cyan. On the other hand, the CBM6 module adopts a common β-sandwich fold, which is colored yellow. c Interdomain interface between GH128 (cyan) and CBM6 (yellow). Residues that participate in forming contacts between the two domains are represented using a stick representation. Hydrogen bonds, indicated by dashed lines, are formed between specific residues with a distance of less than 3.5 Å

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