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. 2023 Jul 24;21:3933–3945. doi: 10.1016/j.csbj.2023.07.024

Fig. 7.

Fig. 7

(A) Crystal structure of BsFrat (2OC6), with highlighted conserved residues in red, conserved antiparallel beta sheet (wheat) and alpha helices (gray). (B) Close Up of conserved antiparallel sheet region (cartoon in wheat), with conserved residues presented as red lines. An additional scheme shows their structural positions in the sheet, according to 2OC6 and the sequence alignment in (C). (C) Results of the multiple sequence alignment of the relevant sequence range, depicted by Berkeley WebLogo. The conserved leucine residue is at alignment position 299, the conserved tyrosine/tryptophan residue at 305, proline at 308 and glycine at 331.