Crystal structures of the myristylated catalytic subunit of camp-dependent protein kinase reveal open and closed conformations. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 May 1994.
Explore 1CMK in 3D Show helices and sheets RCSB PDB PDBe
1CMK 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 | 8-31 | 24 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 1 |
| β-strand | 56-62 | 7 | 1 |
| β-strand | 67-75 | 9 | 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 |
| 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 | 302-306 | 5 | |
| α-helix | 311-312 | 2 | |
| α-helix | 346-349 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-8 | 6 | |
| α-helix | 10-12 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Camp-dependent protein kinase catalytic subunit | E | protein | 350 | Sus scrofa | P36887 (AlphaFold model) |
| cAMP-dependent protein kinase inhibitor, alpha form | I | protein | 22 | Homo sapiens | P61925 (AlphaFold model) |
>1CMK_1 cAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (chains E) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV KHKETGNHFAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVM EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKDGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>1CMK_2 cAMP-dependent protein kinase inhibitor, alpha form (chains I) TTYADFIASGRTGRRNAIHDIL
| ID | Name | Formula | Copies |
|---|---|---|---|
| MYR | Myristic acid | C14 H28 O2 | 1 |
Water and common crystallization additives (IOD) are not listed.
Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Zheng, J., Knighton, D.R., Xuong, N.H. et al. Protein Sci (1993) 2:1559-1573. 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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