Camp-dependent protein kinase, alpha-catalytic subunit in complex with staurosporine. Determined by X-ray diffraction at 2.3 Å resolution. Released 25 Feb 1998.
Explore 1STC in 3D Show helices and sheets RCSB PDB PDBe
1STC contains 21 α-helices and 14 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 | 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 |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 115-121 | 7 | 1 |
| β-strand | 127 | 1 | 3 |
| α-helix | 128-135 | 8 | |
| α-helix | 140-159 | 20 | |
| β-strand | 162-163 | 2 | 4 |
| α-helix | 169-171 | 3 | |
| β-strand | 173-174 | 2 | 3 |
| β-strand | 180-181 | 2 | 3 |
| β-strand | 182 | 1 | 2 |
| β-strand | 189-190 | 2 | 4 |
| β-strand | 195 | 1 | 5 |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 5 |
| α-helix | 218-233 | 16 | |
| α-helix | 243-251 | 9 | |
| α-helix | 263-272 | 10 | |
| α-helix | 277-279 | 3 | |
| α-helix | 289-292 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 302-307 | 6 | |
| α-helix | 311-312 | 2 | |
| α-helix | 328-329 | 2 | |
| α-helix | 331-334 | 4 | |
| α-helix | 344-347 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-13 | 8 | |
| α-helix | 18-20 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Camp-dependent protein kinase | E | protein | 350 | Bos taurus | P00517 (AlphaFold model) |
| Protein kinase inhibitor | I | protein | 20 | P61926 (AlphaFold model) |
>1STC_1 CAMP-DEPENDENT PROTEIN KINASE (chains E) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLV KHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>1STC_2 PROTEIN KINASE INHIBITOR (chains I) TTYADFIASGRTGRRNAIHD
| ID | Name | Formula | Copies |
|---|---|---|---|
| STU | Staurosporine | C28 H26 N4 O3 | 1 |
Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential. Prade, L., Engh, R.A., Girod, A. et al. Structure (1997) 5:1627-1637. DOI 10.1016/S0969-2126(97)00310-9 · 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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