Structure of the mammalian catalytic subunit of camp-dependent protein kinase and an inhibitor peptide displays an open conformation. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 Jan 1994.
Explore 1CTP in 3D Show helices and sheets RCSB PDB PDBe
1CTP contains 17 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 | 8-31 | 24 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-50 | 8 | 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 | 129-135 | 7 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Camp-dependent protein kinase | E | protein | 350 | Sus scrofa | P36887 (AlphaFold model) |
| cAMP-dependent protein kinase inhibitor, alpha form | I | protein | 20 | Homo sapiens | P61926 (AlphaFold model) |
>1CTP_1 cAMP-DEPENDENT PROTEIN KINASE (chains E) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV KHKETGNHFAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVM EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>1CTP_2 cAMP-dependent protein kinase inhibitor, alpha form (chains I) TTYADFIASGRTGRRNAIHD
| ID | Name | Formula | Copies |
|---|---|---|---|
| MYR | Myristic acid | C14 H28 O2 | 1 |
Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation. Karlsson, R., Zheng, J., Xuong, N. et al. Acta Crystallogr D Biol Crystallogr (1993) 49:381-388. DOI 10.1107/S0907444993002306 · PubMed
Other PDB entries of the same protein (UniProt P36887 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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