Fig. 3
From: Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
SgK223 forms a high-affinity dimer. a, b Interaction between αN1, αJ and αK helices and the PsK domain. c Met1363 and Tyr959 side chains are buried within the hydrophobic core at the ‘XX’ dimer interface between αN1 and αJ helices. d Hydrophobic interaction surrounding Leu955 and Leu966 at the dimer interface. αN1, cyan; PK domain, grey; αJ, salmon; αK violet; αL yellow; h-bond and van der Waals interactions are shown in black and red dashed lines, respectively
