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. 2023 Feb 17;15(2):688. doi: 10.3390/pharmaceutics15020688

Figure 1.

Figure 1

Structure of the complex of α-amylase with tendamistat. (A) The crystal structure of tendamistat (PDB accession no. 1OK0). The loop structure that binds to the glycan binding site of α-amylase is highlighted. (B) The crystal structure of the complex with tendamistat bound in the glycan binding site of porcine α-amylase (accession no. 1BVN). (C) Model of the 6-mer loop structure of tendamistat (shaded in red) bound to porcine α-amylase (accession no. 1PIF) generated in silico with CABS-Dock (RMSD = 3.561 Å). The predicted binding energy, ΔG′ = −56 to −60 kJ/mol, is nearly the value calculated from Keq.