PKA double mutant model of PKB in complex with MgATP. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Aug 2003.
Explore 1Q24 in 3D Show helices and sheets RCSB PDB PDBe
1Q24 contains 18 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 | 15-31 | 17 | |
| 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 | 85-97 | 13 | |
| 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 | 243-251 | 9 | |
| α-helix | 263-272 | 10 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-307 | 6 | |
| α-helix | 315-317 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-11 | 6 | |
| β-strand | 22 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent Protein Kinase, alpha-catalytic subunit | A | protein | 350 | Bos taurus | P00517 (AlphaFold model) |
| cAMP-dependent Protein Kinase Inhibitor, alpha form | I | protein | 20 | Q71U53 (AlphaFold model) |
>1Q24_1 cAMP-dependent Protein Kinase, alpha-catalytic subunit (chains A) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV KHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYAPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLMIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>1Q24_2 cAMP-dependent Protein Kinase Inhibitor, alpha form (chains I) TTYADFIASGRTGRRNAIHD
Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT). Gassel, M., Breitenlechner, C.B., Rueger, P. et al. J Mol Biol (2003) 329:1021-1034. DOI 10.1016/S0022-2836(03)00518-7 · PubMed
Other PDB entries of the same protein (UniProt P00517 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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