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. 2019 Oct 25;9:364. doi: 10.3389/fcimb.2019.00364

Figure 1.

Figure 1

BFT-3 structure. (A) BFT structure and active site BFT-3 structure including pro-domain (PD, dark green) and catalytic domain (CD, light green) and zinc-binding site (zinc in purple). (B) Pro-domain residues (ASP190, TYR191, ILE192, ANS193, ASP194, and TYR195) used for defining the BFT-3 binding pocket (light blue) and zinc coordinating residues from the CD (HIS348, HIS352, and HIS358). (C) Chenodeoxycholic acid docked into the BFT-3 zinc-binding site using MOE.