Michaelis-like complex of cAMP-dependent Protein Kinase Catalytic Subunit. Determined by X-ray diffraction at 1.77 Å resolution. Released 16 Dec 2015.
Explore 3X2V in 3D Show helices and sheets RCSB PDB PDBe
3X2V contains 22 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 | 18-31 | 14 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 55-62 | 8 | 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 | |
| α-helix | 334-336 | 3 | |
| α-helix | 345-347 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 606-611 | 6 | |
| α-helix | 618-621 | 4 | |
| β-strand | 622 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase catalytic subunit alpha | A | protein | 357 | Mus musculus | P05132 (AlphaFold model) |
| Substrate Peptide | S | protein | 20 | synthetic construct | P61925 (AlphaFold model) |
>3X2V_1 cAMP-dependent protein kinase catalytic subunit alpha (chains A) HHHHHHMGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGS FGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDN SNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL IDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAA GYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKN HKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
>3X2V_2 Substrate Peptide (chains S) TTYADFIASGRTGRRASIHD
| ID | Name | Formula | Copies |
|---|---|---|---|
| CO3 | Carbonate ion | C O3 | 1 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| MG | Magnesium ion | Mg | 2 |
Protein Kinase A Catalytic Subunit Primed for Action: Time-Lapse Crystallography of Michaelis Complex Formation. Das, A., Gerlits, O., Parks, J.M. et al. Structure (2015) 23:2331-2340. DOI 10.1016/j.str.2015.10.005 · 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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