EC Number   |
Reference |
|---|
   2.7.11.11 | complex between the catalytic subunit and a deletion mutant regulatory subunit RIalpha comprising residues 91-244, structure determination and analysis |
663394 |
| 2.7.11.11 | crystal structure of the protein kinase catalytic subunit with staurosporine bound to the adenosine pocket |
490956 |
| 2.7.11.11 | crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors 1-(5-isoquinolinesulfonyl)-2-methylpiperazine, N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide and N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide |
490955 |
| 2.7.11.11 | crystallization in active conformation |
490800 |
| 2.7.11.11 | crystallization of the muatnt E230Q with MgATP2- and protein kinase inhibitor is only possible as apoenzyme, analysis of the mechanism preventing ternary complex formation by relaxed-complex method |
672647 |
| 2.7.11.11 | hanging drop vapor diffusion method at 4°C |
761455 |
| 2.7.11.11 | hanging drop vapor diffusion method, using 16-23% (v/v) methanol |
737388 |
| 2.7.11.11 | in complex with Mg2+ and beta,gamma-methyleneadenosine 5'-triphosphate, sitting drop vapor diffusion method, using 100 mM MES (pH 6.5), 5 mM dithiothreitol, and 15-20% (w/v) PEG 4000 at 4-14°C |
737679 |
| 2.7.11.11 | modification and computational analysis of the crystal structure of catalytic subunit in complex with two Mg2+ and a phosphorylated substrate peptide, molecular dynamics simulation overview |
677184 |
| 2.7.11.11 | purified myristylated wild-type PKA and a K7C mutant as binary complex with bound substrate SP20 peptide and as ternary complex with bound substrate SP20 peptide and adenosine-5'-(beta,gamma-imido)triphosphate, hanging drop vapor diffusion method, 8-10 mg/ml protein in 50 mM N,N-bis(2-hydroxyethyl)glycine, 150 mM ammonium acetate, and 10 mM DTT, pH 8.0, is combined in 1:10:20:5 molar ratio of protein:AMP-PNP:Mg2+:SP20 for the ternary complex or 1:5 protein:SP20 for the binary complex, screening and method optimization, mixing of equal volumes of protein and well solution, the latter containing 2-18% 2-methyl-2,4-pentanediol, and mother liquor or buffers ranging from pH 5.35 to pH 8.5, 100 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl) propane-1,3-diol, pH 6.5, and 9% MeOH, 8-10 weeks, 4°C, X-ray diffraction structure determination and analysis at 1.35-2.0 A resolution, modeling |
722989 |
