CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.510 | Transferase(Phosphotransferase); domain 1 |
|
1.10.510.10 | Transferase(Phosphotransferase) domain 1 |
Domain Context
CATH Clusters
| Superfamily | Transferase(Phosphotransferase) domain 1 |
| Functional Family | cAMP-dependent protein kinase catalytic subunit alpha |
Enzyme Information
| 2.7.11.11 |
cAMP-dependent protein kinase.
based on mapping to UniProt P36887
ATP + a protein = ADP + a phosphoprotein.
-!- cAMP is required to activate this enzyme. -!- The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits. -!- cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits (i.e. R(2)C(2) + 4 cAMP = R(2)(cAMP)(4) + 2 C). -!- Formerly EC 2.7.1.37.
|
UniProtKB Entries (1)
| P36887 |
KAPCA_PIG
Sus scrofa
CAMP-dependent protein kinase catalytic subunit alpha
|
PDB Structure
| PDB | 1CDK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24).
EMBO J.
|
