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. Author manuscript; available in PMC: 2018 Apr 4.
Published in final edited form as: Int J Biol Macromol. 2016 Nov 16;95:145–152. doi: 10.1016/j.ijbiomac.2016.11.038

Fig. 3. X-ray crystallographic structure of the polyphenol binding pocket of F1Fo ATP synthase.

Fig. 3

α-, β-, and γ-subunits forming an inhibitor binding cavity are shown. Some residues, including αArg-283, are identified. The figure was generated by PDB file 2JJ1 [11] using RasMol software. Residue numbers are based on E. coli numbering.