CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 2 | Mainly Beta | 
|   | 2.60 | Sandwich | 
|   | 2.60.120 | Jelly Rolls | 
|   | 2.60.120.10 | Jelly Rolls | 
Domain Context
CATH Clusters
| Superfamily | Jelly Rolls | 
| Functional Family | cGMP-dependent protein kinase | 
Enzyme Information
| 2.7.11.12 | cGMP-dependent protein kinase. based on mapping to UniProt P00516 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)
| P00516 | KGP1_BOVIN Bos taurus CGMP-dependent protein kinase 1 | 
PDB Structure
| PDB | 3SHR | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Crystal Structure of cGMP-Dependent Protein Kinase Reveals Novel Site of Interchain Communication. Structure | 
