Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | activation loop phosphorylation at Thr197 regulates the enzyme's catalytic activity, molecular mechanism, classical molecular dynamics simulations and ab initio QM/MM calculations are carried out on the wild-type PKA-Mg2+- ATP-substrate complex and its dephosphorylated mutant, T197A, overview | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
R165A | site-directed mutagenesis, the mutant cannot be phosphorylated at Thr197 of the activation loop, molecular dynamics simulations, overview | Homo sapiens |
T197A | site-directed mutagenesis, the side-chain conformations of the P-site Ser in the R165A mutant are similar to that in the wild-type PKA, although the replacement of Arg165 with Ala disconnects the interactions between the pThr 197 and the active site, molecular dynamics simulations, overview | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | PKA-Mg2+-ATP-substrate complex formation and effects on enzyme activity and stability, overview | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | activation loop phosphorylation at Thr197 regulates the enzyme's catalytic activity, molecular mechanism, classical molecular dynamics simulations and ab initio QM/MM calculations are carried out on the wild-type PKA-Mg2+- ATP-substrate complex and its dephosphorylated mutant, T197A, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | phosphorylated residue pThr197 not only facilitates the phosphoryl transfer reaction by stabilizing the transition state through electrostatic interactions but also strongly affects its essential protein dynamics as well as the active site conformation, overview, free energy difference is,1.4 kcal/mol, it is necessary that Asp166 is available as the catalytic base to accept the hydroxyl proton in the late stages of the phosphoryl transfer | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure of the ternary PKA-substrate complex, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
PKA | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | PKA-Mg2+-ATP-substrate complex formation and effects on enzyme activity and stability, overview | Homo sapiens |