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. 2023 May 8;120(20):e2217096120. doi: 10.1073/pnas.2217096120

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Copyright © 2023 the Author(s). Published by PNAS.

This open access article is distributed under Creative Commons Attribution License 4.0 (CC BY).

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Fig. 4. — Lipid-binding pocket of ABD2. (A) Structural superposition of APCDD1 with bound PAM (magenta sticks) from eMBP-APCDD1 chain A and APCDD1 with bound PAM (yellow sticks) from eMBP-APCDD1 chain C. No major conformational changes are observed. The PAM-binding pocket of ABD2 is marked with a red dotted circle. (B) A close-up view of the PAM molecules as shown in (A). (C) The 2|F_O|-|F_C| electron density (blue meshes) of PAM (yellow sticks) from eMBP-APCDD1 chain C contoured at the 0.8 σ level. (D and E) Diagrams of ABD2 and PAM interactions generated with LigPlot+ (30). Panel (D), eMBP-APCDD1 chain A. Panel (E), eMBP-APCDD1 chain C. Atoms are colored as follows: nitrogen, blue; oxygen, red; carbon, black. Hydrogen bonds are displayed as green dashed lines. Red eyelashes denote hydrophobic interactions.