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. 2026 Aug 26;17:1844013. doi: 10.3389/fphar.2026.1844013

FIGURE 4.

Panel pairs A1–E1 display five protein structures in ribbon style with green and orange stick models highlighting active site residues, while panels A2–E2 provide zoomed-in views showing detailed interactions between the green ligands and specific orange-labeled amino acids, each annotated with residue names such as TYR-139, LYS-58, and PHE-134.

Molecular docking between HSP90AA1 and the drugs. (A1) The binding mode of HSP90AA1 and trastuzumab. (B1) The binding mode of HSP90AA1 and lapatinib. (C1) The binding mode of HSP90AA1 and neratinib. (D1) The binding mode of HSP90AA1 and tucatinib. (E1) The binding mode of HSP90AA1 and tanespimycin. (A2), (B2), (C2), (D2) and (E2) represents the enlarged picture of HSP90AA1 and drugs binding, in which the dotted line represents the hydrogen bond, the text part represents the residue name, and the lower right corner represents the atom binding diagram of molecule and protein.