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. Author manuscript; available in PMC: 2017 Apr 15.
Published in final edited form as: ACS Chem Biol. 2016 Feb 10;11(4):1137–1147. doi: 10.1021/acschembio.5b00913

Figure 2.

Figure 2

Overall structure of the BexE dimer and domain organization of the BexE monomer. (A) The BexE dimer (monomer A in green and monomer B in blue). (B) The BexE monomer is composed of three domains: the FAD binding domain (residues 1–169 and 259–372, colored in blue), the middle domain (residues 170–258, colored in green), and the C-terminal domain (373–487, colored in red). (C) A molecular view of the BexE FAD binding site. (D) SA-Fo-Fc omit map contoured at 1.5 σ displaying clear density for FAD in monomer A (left) and monomer B (right).