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. Author manuscript; available in PMC: 2014 Feb 1.
Published in final edited form as: Trends Mol Med. 2012 Dec 5;19(2):74–82. doi: 10.1016/j.molmed.2012.10.011

Figure 3.

Figure 3

Comparison of two GLS1 allosteric inhibitors, BPTES and 968. a. Chemical structure of BPTES. b. Chemical structure of 968. c. X-ray crystallographic structure of human GLS1 bound to BPTES, adapted from [35,36]. Two BPTES molecules are bound at the dimer–dimer interface of the GLS1 tetramer. d. Molecular docking model of 968 to GAC, adapted from [37]. One molecule of 968 is proposed to bind into a hydrophobic pocket formed by the N- and C-termini at the monomer–monomer interface of the GAC dimer.