Additional file 2.

Figure S2.Putative binding pocket identified at the dimer interface in acetokinase family of enzymes. Dimeric interface pocket identified in structurally known members of acetokinase family of enzymes (refer Table‚ÄČ3 of the main article) are shown with cyan spheres. The two substrate binding pockets of the dimeric form are shown in green and blue spheres. Due to continuity between the dimeric interface pocket and the active site cavities of A- and B-subunits in Form-II StAckA, dimeric interface pocket in Form-II is not well defined. StTdcD dimer (A' indicates symmetry relation with A) was generated using the crystallographic 2-fold axis. PDB codes and the subunits used for the analysis are labeled.

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Chittori et al. BMC Structural Biology 2012 12:24   doi:10.1186/1472-6807-12-24