Figure 3. Binding modes of top-performing uncomplexed FLK peptides in the exo-β-(1,3)-glucanase active site. Representative docking poses of FLK4 (cyan), FLK6 (yellow), and FLK13 (brown) within the catalytic pocket of exo-β-(1,3)-glucanase. All three peptides occupy the substrate-binding groove and establish direct contacts with residues lining the catalytic site, illustrating how short, uncomplexed FLK peptides achieve comparable binding through distinct but convergent interaction patterns : Docking-Based Evaluation of Defensin-Derived Peptides and Their Cu²⁺ Complexes as Dual-Target Inhibitors of Exo-β-(1,3)-Glucanase and Penicillin-Binding Protein Transglycosidase 1B : Science and Education Publishing

Figure 3. Binding modes of top-performing uncomplexed FLK peptides in the exo-β-(1,3)-glucanase active site. Representative docking poses of FLK4 (cyan), FLK6 (yellow), and FLK13 (brown) within the catalytic pocket of exo-β-(1,3)-glucanase. All three peptides occupy the substrate-binding groove and establish direct contacts with residues lining the catalytic site, illustrating how short, uncomplexed FLK peptides achieve comparable binding through distinct but convergent interaction patterns

American Journal of Pharmacological Sciences. 2026, 14(1), 7-19 doi:10.12691/ajps-14-1-2