Crystal structure of cAMP-dependent protein kinase catalytic subunit alpha in complex with peptide inhibitor PKI alpha (6-25). Determined by X-ray diffraction at 1.6 Å resolution. Released 4 Aug 2009.
Explore 3FJQ in 3D Show helices and sheets RCSB PDB PDBe
3FJQ contains 19 α-helices and 13 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 | 16-31 | 16 | |
| 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 |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-11 | 6 | |
| α-helix | 20-22 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase catalytic subunit alpha | E | protein | 350 | Mus musculus | P05132 (AlphaFold model) |
| cAMP-dependent protein kinase inhibitor alpha | I | protein | 20 | Mus musculus | P63248 (AlphaFold model) |
>3FJQ_1 cAMP-dependent protein kinase catalytic subunit alpha (chains E) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLV KHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
>3FJQ_2 cAMP-dependent protein kinase inhibitor alpha (chains I) TTYADFIASGRTGRRNAIHD
Comparative surface geometry of the protein kinase family. Thompson, E.E., Kornev, A.P., Kannan, N. et al. Protein Sci (2009) 18:2016-2026. DOI 10.1002/pro.209 · 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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