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. 2021 Nov 3;78(24):8165–8186. doi: 10.1007/s00018-021-04009-z

Fig. 1.

Fig. 1

Structure comparison of B cell-activating and BCR-binding lectins. BambL (from Burkholderia ambifaria, PDB entry 3ZWE), LecB (Pseudomonas aeruginosa, 5A6X), Bc2L-A (B. cenocepacia, 4AOC), and hemagglutinin (H5N1 influenza virus, 2FK0). Proteins are rendered with PyMOL as surface presentations, sugars as sticks, and calcium ions in the binding pockets of LecB and Bc2L-A as green spheres. One monomer per lectin is colored blue. Arrows and numbers mark the approximate distances between individual sugar binding sites. BambL, although the smallest in size, has by far the highest valency