Crystal structure of R336A mutant of cAMP-dependent protein kinase with unphosphorylated turn motif. Determined by X-ray diffraction at 1.8 Å resolution. Released 13 Feb 2013.
Explore 4DG3 in 3D Show helices and sheets RCSB PDB PDBe
4DG3 contains 20 α-helices and 15 β-strands across 2 chains. 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 | 6-11 | 6 | |
| α-helix | 18-21 | 4 | |
| β-strand | 22 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-31 | 17 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 56-62 | 7 | 1 |
| β-strand | 68-75 | 8 | 1 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-95 | 11 | |
| β-strand | 103 | 1 | 2 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 115-121 | 7 | 1 |
| β-strand | 127 | 1 | 2 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 3 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 2 |
| β-strand | 180-182 | 3 | 2 |
| β-strand | 189-190 | 2 | 3 |
| β-strand | 195 | 1 | 4 |
| β-strand | 200 | 1 | 5 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 4 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 263-272 | 10 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
| α-helix | 334-336 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase catalytic subunit alpha | E | protein | 371 | Mus musculus | P05132 (AlphaFold model) |
| cAMP-dependent protein kinase inhibitor alpha | A | protein | 20 | Mus musculus | P63248 (AlphaFold model) |
>4DG3_1 cAMP-dependent protein kinase catalytic subunit alpha (chains E) MGSSHHHHHHSSGLVPRGSHMGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQ LDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVN FPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS LDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAV DWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK RFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIAVSI NEKCGKEFTEF
>4DG3_2 cAMP-dependent protein kinase inhibitor alpha (chains A) TTYADFIASGRTGRRNAIHD
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Turn motif phosphorylation regulates processing of cAMP-dependent protein kinase. Steichen, J.M., Yang, J., Taylor, S.S. To be published.
Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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