PKA RIIbeta holoenzyme with DnaJB1-PKAc fusion in fibrolamellar hepatoceullar carcinoma. Determined by electron microscopy at 6.2 Å resolution. Released 2 Dec 2020.
Explore 6WJG in 3D Show helices and sheets RCSB PDB PDBe
6WJG contains 34 α-helices and 42 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 98-106 | 9 | 1 |
| β-strand | 111-117 | 7 | 1 |
| β-strand | 123-129 | 7 | 1 |
| α-helix | 131-137 | 7 | |
| α-helix | 140-149 | 10 | |
| β-strand | 164-166 | 3 | 1 |
| β-strand | 171-175 | 5 | 1 |
| β-strand | 181-182 | 2 | 2 |
| α-helix | 183-190 | 8 | |
| α-helix | 195-214 | 20 | |
| β-strand | 218 | 1 | 3 |
| β-strand | 228-230 | 3 | 2 |
| β-strand | 234-236 | 3 | 2 |
| β-strand | 244 | 1 | 3 |
| α-helix | 274-285 | 12 | |
| α-helix | 298-306 | 9 | |
| α-helix | 318-326 | 9 | |
| α-helix | 357-361 | 5 | |
| α-helix | 370-372 | 3 | |
| α-helix | 383-384 | 2 | |
| α-helix | 400-402 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 98-107 | 10 | 4 |
| β-strand | 110-117 | 8 | 4 |
| β-strand | 123-128 | 6 | 4 |
| α-helix | 132-137 | 6 | |
| α-helix | 140-150 | 11 | |
| β-strand | 164-166 | 3 | 4 |
| β-strand | 171-176 | 6 | 4 |
| α-helix | 183-190 | 8 | |
| α-helix | 195-214 | 20 | |
| β-strand | 218 | 1 | 5 |
| β-strand | 228-229 | 2 | 6 |
| β-strand | 235-236 | 2 | 6 |
| β-strand | 244 | 1 | 5 |
| β-strand | 256 | 1 | 7 |
| β-strand | 259 | 1 | 7 |
| α-helix | 262-265 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 279-285 | 7 | |
| α-helix | 298-306 | 9 | |
| α-helix | 318-327 | 10 | |
| α-helix | 357-361 | 5 | |
| α-helix | 366-367 | 2 | |
| α-helix | 370-373 | 4 | |
| α-helix | 385-387 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 114 | 1 | 8 |
| α-helix | 137-148 | 12 | |
| α-helix | 152-154 | 3 | |
| α-helix | 158-167 | 10 | |
| β-strand | 169-173 | 5 | 9 |
| β-strand | 185 | 1 | 10 |
| α-helix | 186 | 1 | |
| β-strand | 191-192 | 2 | 9 |
| β-strand | 199-202 | 4 | 11 |
| β-strand | 207-211 | 5 | 11 |
| β-strand | 227 | 1 | 8 |
| β-strand | 229 | 1 | 10 |
| β-strand | 234 | 1 | 11 |
| β-strand | 240-244 | 5 | 9 |
| α-helix | 247-264 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 137-147 | 11 | |
| α-helix | 151-154 | 4 | |
| α-helix | 158-166 | 9 | |
| β-strand | 170-173 | 4 | 12 |
| β-strand | 182 | 1 | 13 |
| β-strand | 184 | 1 | 13 |
| β-strand | 185-186 | 2 | 14 |
| β-strand | 188-191 | 4 | 12 |
| β-strand | 196-202 | 7 | 15 |
| β-strand | 207-209 | 3 | 15 |
| β-strand | 213-214 | 2 | 15 |
| α-helix | 221-224 | 4 | |
| β-strand | 228-229 | 2 | 14 |
| β-strand | 233-236 | 4 | 15 |
| β-strand | 240-246 | 7 | 12 |
| α-helix | 247-264 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DnaJ homolog subfamily B member 1, cAMP-dependent protein kinase catalytic subunit alpha fusion | A, B | protein | 405 | Homo sapiens | P17612 (AlphaFold model), P25685 (AlphaFold model) |
| cAMP-dependent protein kinase type II-beta regulatory subunit | C, D | protein | 416 | Rattus norvegicus | P12369 (AlphaFold model) |
>6WJG_1 DnaJ homolog subfamily B member 1, cAMP-dependent protein kinase catalytic subunit alpha fusion (chains A, B) GKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKR EIFDRYGEEVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKET GNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPG GEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDF GFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKGVDWWALGVLIYEMAAGYPPFFADQPIQ IYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAI YQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>6WJG_2 cAMP-dependent protein kinase type II-beta regulatory subunit (chains C, D) MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGD AGAAAGGGTPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNP DEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVI DQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPG ALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQ IIAQGDSADSFFIVESGEVRITMKRKGKSDIEENGAVEIARCLRGQYFGELALVTNKPRA ASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA
Structural analyses of the PKA RII beta holoenzyme containing the oncogenic DnaJB1-PKAc fusion protein reveal protomer asymmetry and fusion-induced allosteric perturbations in fibrolamellar hepatocellular carcinoma. Lu, T.W., Aoto, P.C., Weng, J.H. et al. PLoS Biol (2020) 18:e3001018-e3001018. DOI 10.1371/journal.pbio.3001018 · PubMed
Other PDB entries of the same protein (UniProt P17612 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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