Fig. 4

Crystal structure of ZmDRIK1 apo form. a Cartoon representation of the ZmDRIK1-KD structure in the apo form. Structure features: glycine-rich (P-loop – cyan; hinge region – yellow; catalytic loop -pink; DLE (more commonly DFG) motif – blue; activation segment – orange; C-helix – purple. Other protein regions are in green. b Closer look at the ATP binding pocket. Amino acids important for ATP binding and pocket stabilization are shown as stick (carbon in yellow; oxygen in red; nitrogen in blue) and the interaction between them in red dashed lines. Surface of amino acids Leu²⁴⁰, Tyr³⁶³ and Leu³⁷⁵ are shown in light orange. (c and f) Catalytic pocket of apo ZmDRIK1-KD (PDB: 6CPY). Leu²⁴⁰; Tyr³⁶³ and Leu³⁷⁵ are shown as sticks, and the surfaces of these amino acids are colored green, blue and red, respectively. (d and g) Catalytic pocket of CARK1 cocrystallized with AMP-PNP (PDB: 5XD6). AMP-PNP is represented in stick, and atoms are colored as follows: carbon – green; nitrogen – blue; oxygen - red; phosphate – orange. (e and h) Superposition of the ZmDRIK1 ATP binding site with AMP-PNP from the CARK1 structure. The protein molecular surface is shown in white with 50% transparency