Function and Biology Details
Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Cyclic nucleotide-binding domain
- Cyclic nucleotide-binding, conserved site
- Cyclic nucleotide-binding domain superfamily
- cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain
- Protein kinase domain
- RmlC-like jelly roll fold
- Protein kinase, ATP binding site
- Serine/threonine-protein kinase, active site
4 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase type II-beta regulatory subunit
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 46.27 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Jelly Rolls
Length: 416 amino acids
Theoretical weight: 46.27 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P31324 (Residues: 1-416; Coverage: 100%)
Sequence domains:
Structure domains: Jelly Rolls
cAMP-dependent protein kinase catalytic subunit alpha
Molecule details ›
Chain: B
Length: 350 amino acids
Theoretical weight: 40.74 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein kinase domain
Structure domains:
Length: 350 amino acids
Theoretical weight: 40.74 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: P05132 (Residues: 2-351; Coverage: 100%)
Sequence domains: Protein kinase domain
Structure domains:
