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For clarity, only six protomers are revealed in surface area representation and 3 are demonstrated in cartoon representation to illustrate the special interfaces.
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-autophosphorylation exactly where T446 concurrently interacts with the carboxylate of the catalytic aspartate D414 plus the γ-phosphate of ATP. As depicted within a two-dimensional distance histogram, the dimer predominantly populates states inconsistent with trans
having said that, this dimer geometry spots the two active sites distant from the dimer interface and is also incompatible with data demonstrating that this reaction can manifest in trans
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The nucleotide, totally free phosphate, and vital facet chains are rendered as sticks. The Mg2+ is indicated to be a sphere. Hydrogen bond and salt-bridge interactions in the unphosphorylated kinase are denoted as dotted traces. The R-backbone is demonstrated in surface area representation. A superposition of all 3 chains with the unphosphorylated enzyme with phosphorylated PKR kinase domain is shown in Figure S2.
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Relative for the Cʹ protomer, the B protomer is rotated by 38°. The bound nucleotide in chain C is depicted in adhere representation. B) Detailed look at from the more info interactions stabilizing the interface. The orientation corresponds to the 90° rotation from the framework depicted partially A. important facet chain and main chain atoms are rendered as sticks. Hydrogen bond and salt-bridge interactions are denoted by dashed traces.
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