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. 2010 Feb 18;5(2):e8943. doi: 10.1371/journal.pone.0008943

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Krishnamoorthy et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Inline graphic — (A) and (B) compares the published and current docked models of BH3I-1 on , respectively. In the published model, the stoichiometry was constrained to a single site, so the ligand preferred the site in between the two adjacent pockets. The key residues that interact with BH3I-1 within 5 are highlighted in orange. In the current model, two BH3I-1 molecules bind adjacent to each other with distinctive affinities. Site A and B are circled and highlighted in yellow and red color, respectively.

(A) and (B) compares the published and current docked models of BH3I-1 on , respectively. In the published model, the stoichiometry was constrained to a single site, so the ligand preferred the site in between the two adjacent pockets. The key residues that interact with BH3I-1 within 5 are highlighted in orange. In the current model, two BH3I-1 molecules bind adjacent to each other with distinctive affinities. Site A and B are circled and highlighted in yellow and red color, respectively.