Function and Biology Details
Reaction catalysed:
[(1) L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)., (2) L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP +H(+).]
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132590 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase catalytic subunit alpha
Molecule details ›
Chain: A
Length: 351 amino acids
Theoretical weight: 40.83 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein kinase domain
Structure domains:
Length: 351 amino acids
Theoretical weight: 40.83 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
- Canonical:
P00517 (Residues: 1-351; Coverage: 100%)
Sequence domains: Protein kinase domain
Structure domains:
cAMP-dependent protein kinase inhibitor alpha
Molecule details ›
Chain: I
Length: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P61925 (Residues: 6-25; Coverage: 26%)
