Regulatory subunit of camp dependent protein kinase. Determined by X-ray diffraction at 2.8 Å resolution. Released 7 Dec 1996.
Explore 1RGS in 3D Show helices and sheets RCSB PDB PDBe
1RGS contains 13 α-helices and 17 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 121-132 | 12 | |
| α-helix | 134-136 | 3 | |
| α-helix | 141-150 | 10 | |
| β-strand | 152-156 | 5 | 1 |
| β-strand | 161-163 | 3 | 2 |
| β-strand | 171-177 | 7 | 1 |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 190-192 | 3 | 2 |
| β-strand | 197-198 | 2 | 1 |
| α-helix | 200-205 | 6 | |
| β-strand | 212-215 | 4 | 2 |
| β-strand | 219-225 | 7 | 1 |
| α-helix | 226-228 | 3 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-250 | 17 | |
| α-helix | 252-256 | 5 | |
| α-helix | 259-268 | 10 | |
| β-strand | 270 | 1 | 3 |
| β-strand | 273-274 | 2 | 3 |
| β-strand | 279-281 | 3 | 4 |
| β-strand | 289-295 | 7 | 3 |
| β-strand | 298-302 | 5 | 4 |
| β-strand | 311-316 | 6 | 4 |
| β-strand | 321-322 | 2 | 3 |
| α-helix | 324-329 | 6 | |
| β-strand | 336-339 | 4 | 4 |
| β-strand | 343-349 | 7 | 3 |
| α-helix | 350-356 | 7 | |
| α-helix | 361-365 | 5 | |
| α-helix | 368-370 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Camp dependent protein kinase | A | protein | 288 | Bos taurus | P00514 (AlphaFold model) |
>1RGS_1 CAMP DEPENDENT PROTEIN KINASE (chains A) RRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAM FPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAA TVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEP VQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNR PRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
| ID | Name | Formula | Copies |
|---|---|---|---|
| CMP | Adenosine-3',5'-cyclic-monophosphate | C10 H12 N5 O6 P | 2 |
Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains. Su, Y., Dostmann, W.R., Herberg, F.W. et al. Science (1995) 269:807-813. PubMed
Other PDB entries of the same protein (UniProt P00514 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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