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. Author manuscript; available in PMC: 2013 Sep 11.
Published in final edited form as: Angew Chem Int Ed Engl. 2011 Nov 21;51(5):1124–1137. doi: 10.1002/anie.201103110

Figure 6.

Figure 6

Structures and dynamics of the ζ prenyl transferase UPPS. a) Overall structure of a bisphosphonate-bound E. coli UPPS monomer. b) substrates (FPP and IPP) bound to UPPS active site. c) Structural alignment of the predicted structure of Rv3378c with UPPS. d) Molecular dynamics simulation of UPPS. Black, data taken every 10 ps; grey, every 100 ps. e) frequency of occurence of pocket versus pocket volume. The apo structure has a small pocket volume; the largest volume is close to that occupied by a large inhibitor.