CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.30 | Roll |
|
2.30.29 | PH-domain like |
|
2.30.29.30 | Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) |
Domain Context
CATH Clusters
| Superfamily | Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) |
| Functional Family | G protein-coupled receptor kinase |
Enzyme Information
| 2.7.11.15 |
[Beta-adrenergic-receptor] kinase.
based on mapping to UniProt P25098
ATP + [beta-adrenergic receptor] = ADP + [beta-adrenergic receptor] phosphate.
-!- Acts on the agonist-occupied form of the receptor; also phosphorylates rhodopsin, but more slowly. -!- Does not act on casein or histones. -!- Inhibited by Zn(2+) and digitonin but is unaffected by cyclic-AMP (cf. EC 2.7.11.14 and EC 2.7.11.16). -!- Formerly EC 2.7.1.126.
|
UniProtKB Entries (2)
| P62871 |
GBB1_BOVIN
Bos taurus
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
|
| P25098 |
ARBK1_HUMAN
Homo sapiens
Beta-adrenergic receptor kinase 1
|
PDB Structure
| PDB | 6C2Y |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Utilizing a structure-based docking approach to develop potent G protein-coupled receptor kinase (GRK) 2 and 5 inhibitors.
Bioorg. Med. Chem. Lett.
|
