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EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate - -
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate activation involves the activation loop, a polypeptide region outside the active site cleft, which is reversibly phosphorylated at Thr197, phosphorylation leads to enzyme inhibition, activation mechanism, overview 490931
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate activation mechanism 661135, 663349
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate active site residues and structure, mechanism of ligand binding and ligand-induced conformational changes 662608
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism 661314
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism, active site structure, Tyr204 is required and involved in the hydrophobic network, substrate-induced interaction of Tyr204 and Asp166, overview 662614
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic site structure, Asp166 is the catalytic base invariant in all kinases, activation mechanism, overview 490800
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate conserved residues K336 and H338 are important for catalytic activity, R324 is important in substrate binding 673866
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate phosphoryltransfer mechanism, substrate-binding site structure, the phosphorylated Thr197 in the catalytic subunit of cAMP-dependent protein is essential for activity, overview 677184
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate random kinetic mechanism, active site structure with key residues E91, K72, N171, K168, the general base catalyst D166, and essential catalytic D184, overview, reaction mechanism 490935
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