A complex structure between the Catalytic and Regulatory subunit of Protein Kinase A that represents the inhibited state. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Nov 2007.
Explore 2QCS in 3D Show helices and sheets RCSB PDB PDBe
2QCS contains 31 α-helices and 31 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 | 14-31 | 18 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-51 | 9 | 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 |
| α-helix | 122 | 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 | 199-200 | 2 | 5 |
| α-helix | 202-204 | 3 | |
| α-helix | 207-210 | 4 | |
| β-strand | 215 | 1 | 4 |
| α-helix | 219-233 | 15 | |
| 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 | 94-97 | 4 | |
| β-strand | 98-99 | 2 | 5 |
| α-helix | 105-109 | 5 | |
| α-helix | 120-129 | 10 | |
| α-helix | 134-137 | 4 | |
| α-helix | 141-150 | 10 | |
| β-strand | 152-156 | 5 | 6 |
| β-strand | 161-163 | 3 | 7 |
| β-strand | 168 | 1 | 8 |
| α-helix | 169 | 1 | |
| β-strand | 171-177 | 7 | 6 |
| β-strand | 180-184 | 5 | 7 |
| β-strand | 187-192 | 6 | 7 |
| β-strand | 197-198 | 2 | 6 |
| α-helix | 200-203 | 4 | |
| β-strand | 208 | 1 | 8 |
| β-strand | 212-215 | 4 | 7 |
| β-strand | 219-225 | 7 | 6 |
| α-helix | 226-249 | 24 | |
| α-helix | 252-254 | 3 | |
| α-helix | 259-268 | 10 | |
| β-strand | 270-274 | 5 | 9 |
| β-strand | 279-281 | 3 | 9 |
| β-strand | 289-303 | 15 | 9 |
| β-strand | 310-316 | 7 | 9 |
| β-strand | 321-322 | 2 | 9 |
| α-helix | 325-327 | 3 | |
| β-strand | 336-349 | 14 | 9 |
| α-helix | 350-357 | 8 | |
| α-helix | 360-364 | 5 | |
| α-helix | 368-374 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase, alpha-catalytic subunit | A | protein | 350 | Mus musculus | P05132 (AlphaFold model) |
| cAMP-dependent protein kinase type I-alpha regulatory subunit | B | protein | 291 | Bos taurus | P00514 (AlphaFold model) |
>2QCS_1 cAMP-dependent protein kinase, alpha-catalytic subunit (chains A) GNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLV KHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVM EYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYI QVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATT DWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
>2QCS_2 cAMP-dependent protein kinase type I-alpha regulatory subunit (chains B) KGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFD AMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPR AATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADAL EPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLM NRPKAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSVA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
| TAM | Tris(hydroxyethyl)aminomethane | C7 H17 N O3 | 1 |
Water and common crystallization additives (SO4, ACT, GOL) are not listed.
PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation. Kim, C., Cheng, C.Y., Saldanha, S.A. et al. Cell (2007) 130:1032-1043. DOI 10.1016/j.cell.2007.07.018 · PubMed
Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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