Structure of cAMP-dependent protein kinase using a MD-MX procedure, produced using 1.63 Angstrom data. Determined by X-ray diffraction at 1.63 Å resolution. Released 7 Dec 2022.
Explore 7V0G in 3D Show helices and sheets RCSB PDB PDBe
7V0G 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 | 17-31 | 15 | |
| 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 | 277-279 | 3 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-312 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-11 | 6 | |
| α-helix | 18-21 | 4 | |
| β-strand | 22 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase catalytic subunit alpha | E | protein | 350 | Mus musculus | P05132 (AlphaFold model) |
| Peptide from cAMP-dependent protein kinase inhibitor alpha | I | protein | 19 | Homo sapiens | P61925 (AlphaFold model) |
>7V0G_1 cAMP-dependent protein kinase catalytic subunit alpha (chains E) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLV KHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
>7V0G_2 Peptide from cAMP-dependent protein kinase inhibitor alpha (chains I) TTYADFIASGRTGRRNAIH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| PO4 | Phosphate ion | O4 P | 2 |
| MG | Magnesium ion | Mg | 2 |
Molecular-dynamics simulation methods for macromolecular crystallography. Wych, D.C., Aoto, P.C., Vu, L. et al. Acta Crystallogr D Struct Biol (2023) 79:50-65. DOI 10.1107/S2059798322011871 · PubMed
Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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