Crystallization (Comment) | Organism |
---|---|
crystallization of the muatnt E230Q with MgATP2- and protein kinase inhibitor is only possible as apoenzyme, analysis of the mechanism preventing ternary complex formation by relaxed-complex method | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
E230Q | site-directed mutagenesis of the catalytic subunit, the mutation affects the local structure of the the F-to-G helix loop and asp241, and the binding of protein kinase inhibitor PKI, the mutant protein can only be crystallizes as apoenzyme | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
protein kinase inhibitor PKI | binding structure, overview | Mus musculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | P05132 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + kemptide | - |
Mus musculus | ADP + phospho-kemptide | - |
? | |
additional information | the catalytic subunit has a cluster of nonconserved acidic residues, Glu127, Glu170, Glu203, Glu230, and Asp241, that are crucial for substrate recognition and binding | Mus musculus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the catalytic subunit has a cluster of nonconserved acidic residues, Glu127, Glu170, Glu203, Glu230, and Asp241, that are crucial for substrate recognition and binding, protein dynamics of the catalytic C-subunit, overview | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
PKA | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mus musculus |