Reaction Details |
| Report a problem with these data |
Target | cAMP-dependent protein kinase catalytic subunit alpha |
---|
Ligand | BDBM15211 |
---|
Substrate/Competitor | BDBM27221 |
---|
Meas. Tech. | Fluorescence Polarization-Based Binding Displacement Kinase Assay |
---|
pH | 7.5±n/a |
---|
Temperature | 303.15±n/a K |
---|
Kd | 23±2 nM |
---|
Citation | Lavogina, D; Lust, M; Viil, I; König, N; Raidaru, G; Rogozina, J; Enkvist, E; Uri, A; Bossemeyer, D Structural analysis of ARC-type inhibitor (ARC-1034) binding to protein kinase A catalytic subunit and rational design of bisubstrate analogue inhibitors of basophilic protein kinases. J Med Chem52:308-21 (2009) [PubMed] Article |
---|
More Info.: | Get all data from this article, Inhibition_Run data, Solution Info, Assay Method |
---|
|
cAMP-dependent protein kinase catalytic subunit alpha |
---|
Name: | cAMP-dependent protein kinase catalytic subunit alpha |
Synonyms: | KAPCA_MOUSE | PKA C-alpha | Pkaca | Prkaca | cAMP-Dependent Protein Kinase (PKA) | cAMP-dependent protein kinase catalytic subunit alpha | cAMP-dependent protein kinase, alpha-catalytic subunit |
Type: | Enzyme Catalytic Unit |
Mol. Mass.: | 40579.18 |
Organism: | Mus musculus (mouse) |
Description: | n/a |
Residue: | 351 |
Sequence: | MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVML
VKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
|
|
|
BDBM15211 |
---|
BDBM27221 |
---|
Name | BDBM15211 |
Synonyms: | CHEMBL104264 | H-89 | H89 | HT-89 (H-89) | N-(2-{[(2E)-3-(4-bromophenyl)prop-2-en-1-yl]amino}ethyl)isoquinoline-5-sulfonamide | N-[2-[[(E)-3-(4-bromophenyl)prop-2-enyl]amino]ethyl]isoquinoline-5-sulfonamide |
Type | Small organic molecule |
Emp. Form. | C20H20BrN3O2S |
Mol. Mass. | 446.361 |
SMILES | Brc1ccc(\C=C\CNCCNS(=O)(=O)c2cccc3cnccc23)cc1 |
Structure |
|