cAMP-dependent protein kinase PKA catalytic subunit with PKI-5-24. Determined by X-ray diffraction at 1.87 Å resolution. Released 23 May 2006.
Explore 2GFC in 3D Show helices and sheets RCSB PDB PDBe
2GFC contains 19 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 | 43-50 | 8 | 1 |
| β-strand | 56-62 | 7 | 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 | 243-252 | 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 | 6-12 | 7 | |
| α-helix | 18-21 | 4 | |
| 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 | I | protein | 20 | P61926 (AlphaFold model) |
>2GFC_1 cAMP-dependent protein kinase, alpha-catalytic subunit (chains A) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV KHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>2GFC_2 cAMP-dependent protein kinase inhibitor alpha (chains I) TTYADFIASGRTGRRNAIHD
| ID | Name | Formula | Copies |
|---|---|---|---|
| OCT | N-octane | C8 H18 | 1 |
Structural Analysis of Protein Kinase A Mutants with Rho-kinase Inhibitor Specificity. Bonn, S., Herrero, S., Breitenlechner, C.B. et al. J Biol Chem (2006) 281:24818-24830. DOI 10.1074/jbc.M512374200 · 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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