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Fig. 1 | BMC Molecular and Cell Biology

Fig. 1

From: Glutantβase: a database for improving the rational design of glucose-tolerant β-glucosidases

Fig. 1

Glutantβase’s interface overview. (a) Protein’s details and three-dimensional visualization (for this example, we used the β-glucosidase of Streptomyces sp. Root1295 - UniProt ID: A0A0Q7I6P6). (b) Protein sequence. Some amino acids are colored according to their predicted role: (c) secondary structure (border-bottom is colored of yellow for an alpha-helix region, purple for a β-strand region, and grey for a loop region); (d) predicted mutation (green); (e) residue located in the substrate channel (orange letters); (f) amino acids conserved in more than 80% of the GH1 β-glucosidases (red); (g) amino acids conserved in more than 50% of the GH1 β-glucosidases (blue); (h) amino acids present in the coevolution network (border-top is colored of magenta for community 1 and colored of cyan for community 2; a click on the button shows details about correlated residues); and (i) acid/base catalytic or nucleophile (black)

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