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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: Curr Opin Struct Biol. 2009 Nov 14;19(6):650–657. doi: 10.1016/j.sbi.2009.10.017

Fig. 3. Inhibitor complex of a PknB KD mutant resembled an autophosphorylation complex.

Fig. 3

A. PknB monomers formed an asymmetric offset dimer with contacts between the G-helices. Identical interface residues occur in distinct environments in the presumptive substrate (yellow) and enzymatic (blue). The activation loop was disordered in the substrate KD (yellow dashed line) and ordered (red line) in the enzyme KD.) B. Surface representation showing the contacts between kinase molecules and the ordered activation loop (red) in the enzyme KD.