cAMP-dependent protein kinase A catalytic domain in complex with voltage gated calcium channel peptide ternary complex 1. Determined by X-ray diffraction at 2.85 Å resolution. Released 11 Dec 2024.
Explore 8UKP in 3D Show helices and sheets RCSB PDB PDBe
8UKP contains 19 α-helices and 17 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 | 1973-1975 | 3 | |
| β-strand | 1982-1983 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-31 | 15 | |
| β-strand | 43-51 | 9 | 2 |
| β-strand | 55-62 | 8 | 2 |
| β-strand | 67-74 | 8 | 2 |
| β-strand | 75 | 1 | 3 |
| α-helix | 76-81 | 6 | |
| α-helix | 85-97 | 13 | |
| β-strand | 103 | 1 | 4 |
| α-helix | 104-105 | 2 | |
| β-strand | 106-111 | 6 | 2 |
| β-strand | 115 | 1 | 3 |
| β-strand | 116-120 | 5 | 2 |
| β-strand | 127 | 1 | 4 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 5 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 4 |
| α-helix | 175 | 1 | |
| β-strand | 180-182 | 3 | 4 |
| β-strand | 189-190 | 2 | 5 |
| β-strand | 195 | 1 | 6 |
| β-strand | 199-200 | 2 | 1 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 6 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-252 | 10 | |
| α-helix | 256-258 | 3 | |
| α-helix | 263-272 | 10 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-307 | 6 | |
| α-helix | 344-347 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Arg-gly-phe-leu-arg-ser-ala-ser-leu-gly-arg-arg-ala-ser-phe-his-leu | C | protein | 17 | Homo sapiens | Q13936 (AlphaFold model) |
| cAMP-dependent protein kinase catalytic subunit alpha | E | protein | 339 | Mus musculus | P05132 (AlphaFold model) |
>8UKP_1 ARG-GLY-PHE-LEU-ARG-SER-ALA-SER-LEU-GLY-ARG-ARG-ALA-SER-PHE-HIS-LEU (chains C) RGFLRSASLGRRASFHL
>8UKP_2 cAMP-dependent protein kinase catalytic subunit alpha (chains E) SNAVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAM KILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSH LRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRV KGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIV SGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVE APFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Crystallographic, kinetic, and calorimetric investigation of PKA interactions with L-type calcium channels and Rad GTPase. Yoo, R., Haji-Ghassemi, O., Bader, M. et al. J Biol Chem (2024) 301:108039-108039. DOI 10.1016/j.jbc.2024.108039 · PubMed
Other PDB entries of the same protein (UniProt Q13936 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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