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. 2024 Aug 21;52(18):11301–11316. doi: 10.1093/nar/gkae703

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© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Structural basis for dual modes of pP1192R inhibition by m-AMSA. (A) Structural superimposition of Site 1 and Site 2. The two protomers are pink and yellow, with m-AMSA red in Site 1 and blue in Site 2. The key residues involved in m-AMSA–pP1192R interaction are shown as sticks. (B and D) Detailed view of drug-protein interaction at Site 1 (B) and Site 2 (D). Key residues involved in m-AMSA-pP1192R interaction are shown and labelled. Mg²⁺ ions are depicted as spheres. (C and E) LigPlot analysis of drug-protein interaction at Site 1 (C) and Site 2 (E). The residue E438, which is involved in hydrogen bonding, is shown as a sphere and a stick, and the amino acids that differ at the two interaction sites are circled in red. (F) Structural superimposition of m-AMSA-binding sites in human Topo IIβ (PDB code: 4G0U) and pP1192R (Site 1).