ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with the C-terminal PIF domain of OXI1/AGC2-1. Membrane-associated after cell stimulation leading to its translocation. The PH domain is responsible for the interaction with the 3-phosphoinositides. The activation loop within the kinase domain is the target of phosphorylation. The PIF-binding region on the kinase domain of PDK2 acts as a docking site, enabling it to interact with and enhance the phosphorylation of substrates containing the PIF motif (By similarity). The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors. Phosphorylation on Thr-212 in the activation loop is required for full activity. PDK2 itself can autophosphorylate Thr-212, leading to its own activation (By similarity). Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily. Truncated N-terminus. Truncated N-terminus.