CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.5 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
1.20.5.170 |
Domain Context
CATH Clusters
| Superfamily | 1.20.5.170 |
| Functional Family | cGMP-dependent protein kinase 1 |
Enzyme Information
| 2.7.11.12 |
cGMP-dependent protein kinase.
based on mapping to UniProt Q13976
ATP + a protein = ADP + a phosphoprotein.
-!- cGMP is required to activate this enzyme. -!- The enzyme occurs as a dimer in higher eukaryotes. -!- The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. -!- This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates. -!- The enzyme also has two allosteric cGMP-binding sites (sites A and B). -!- Binding of cGMP causes a conformational change that is associated with activation of the kinase. -!- Formerly EC 2.7.1.37.
|
UniProtKB Entries (1)
| Q13976 |
KGP1_HUMAN
Homo sapiens
CGMP-dependent protein kinase 1
|
PDB Structure
| PDB | 3NMD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring.
J.Biol.Chem.
|