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Literature summary for 2.7.11.11 extracted from

  • Jin, H.; Wu, T.; Jiang, Y.; Zou, J.; Zhuang, S.; Mao, X.; Yu, Q.
    Role of phosphorylated Thr-197 in the catalytic subunit of cAMP-dependent protein kinase (2007), Theochem, 805, 9-15.
No PubMed abstract available
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Crystallization (Commentary)

Crystallization (Comment) Organism
modification and computational analysis of the crystal structure of catalytic subunit in complex with two Mg2+ and a phosphorylated substrate peptide, molecular dynamics simulation overview Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + 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 Mus musculus
a

Synonyms

Synonyms Comment Organism
PKA
-
 Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mus musculus