The structure of the IL-11 signalling complex, with full-length extracellular gp130. Determined by electron microscopy at 4.0 Å resolution. Released 29 Nov 2023.
Explore 8DPT in 3D Show helices and sheets RCSB PDB PDBe
8DPT contains 70 α-helices and 114 β-strands across 6 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 | 8-10 | 3 | 1 |
| β-strand | 15-17 | 3 | 2 |
| β-strand | 22-27 | 6 | 1 |
| α-helix | 30-36 | 7 | |
| α-helix | 40-42 | 3 | |
| β-strand | 43-47 | 5 | 3 |
| β-strand | 50-51 | 2 | 3 |
| α-helix | 52-53 | 2 | |
| α-helix | 54-56 | 3 | |
| β-strand | 57-61 | 5 | 1 |
| β-strand | 64-69 | 6 | 1 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 91-97 | 7 | 3 |
| β-strand | 99-101 | 3 | 2 |
| α-helix | 103-107 | 5 | |
| β-strand | 108-113 | 6 | 4 |
| β-strand | 114-115 | 2 | 5 |
| β-strand | 121-125 | 5 | 4 |
| β-strand | 135-142 | 8 | 6 |
| β-strand | 145-146 | 2 | 6 |
| α-helix | 147-149 | 3 | |
| β-strand | 150-151 | 2 | 6 |
| α-helix | 152-153 | 2 | |
| β-strand | 159-161 | 3 | 4 |
| β-strand | 172-180 | 9 | 6 |
| β-strand | 183-186 | 4 | 6 |
| α-helix | 187-189 | 3 | |
| β-strand | 190-192 | 3 | 6 |
| α-helix | 194-197 | 4 | |
| β-strand | 198-199 | 2 | 5 |
| α-helix | 200-203 | 4 | |
| β-strand | 204-209 | 6 | 7 |
| β-strand | 218-223 | 6 | 7 |
| α-helix | 226-229 | 4 | |
| β-strand | 233-241 | 9 | 8 |
| β-strand | 248-249 | 2 | 8 |
| α-helix | 252-255 | 4 | |
| β-strand | 261-264 | 4 | 7 |
| α-helix | 267-268 | 2 | |
| β-strand | 272-281 | 10 | 8 |
| α-helix | 288-291 | 4 | |
| β-strand | 295-298 | 4 | 8 |
| α-helix | 299-301 | 3 | |
| α-helix | 307-309 | 3 | |
| β-strand | 310-316 | 7 | 9 |
| β-strand | 323-329 | 7 | 9 |
| α-helix | 331-333 | 3 | |
| α-helix | 334-337 | 4 | |
| β-strand | 343-350 | 8 | 10 |
| β-strand | 356-360 | 5 | 10 |
| β-strand | 364-369 | 6 | 9 |
| β-strand | 374-381 | 8 | 10 |
| β-strand | 386 | 1 | 10 |
| α-helix | 387-389 | 3 | |
| β-strand | 390-393 | 4 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-42 | 27 | |
| α-helix | 55-56 | 2 | |
| α-helix | 69-93 | 25 | |
| α-helix | 96-101 | 6 | |
| α-helix | 104-125 | 22 | |
| α-helix | 128-132 | 5 | |
| α-helix | 134-143 | 10 | |
| α-helix | 146-175 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-16 | 3 | 11 |
| β-strand | 22-25 | 4 | 12 |
| β-strand | 35-39 | 5 | 11 |
| β-strand | 42 | 1 | 11 |
| α-helix | 44-46 | 3 | |
| β-strand | 56-59 | 4 | 12 |
| α-helix | 64-66 | 3 | |
| β-strand | 68-74 | 7 | 11 |
| β-strand | 79-87 | 9 | 11 |
| α-helix | 90-94 | 5 | |
| β-strand | 95-99 | 5 | 13 |
| β-strand | 107-111 | 5 | 13 |
| β-strand | 121-128 | 8 | 14 |
| β-strand | 157-159 | 3 | 13 |
| β-strand | 168-177 | 10 | 14 |
| β-strand | 180-181 | 2 | 14 |
| β-strand | 184-189 | 6 | 14 |
| α-helix | 190-193 | 4 | |
| α-helix | 196-199 | 4 | |
| β-strand | 200-206 | 7 | 15 |
| β-strand | 214-219 | 6 | 15 |
| β-strand | 232-240 | 9 | 16 |
| β-strand | 247-249 | 3 | 16 |
| β-strand | 255-258 | 4 | 15 |
| α-helix | 261-262 | 2 | |
| β-strand | 267-275 | 9 | 16 |
| α-helix | 282-288 | 7 | |
| β-strand | 289-291 | 3 | 16 |
| α-helix | 293-295 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-6 receptor subunit beta | A, D | protein | 591 | Homo sapiens | P40189 (AlphaFold model) |
| Interleukin-11 | B, E | protein | 169 | Homo sapiens | P20809 (AlphaFold model) |
| Interleukin-11 receptor subunit alpha | C, F | protein | 298 | Homo sapiens | Q14626 (AlphaFold model) |
>8DPT_1 Interleukin-6 receptor subunit beta (chains A, D) GELLDPCGYISPESPVVQLHSNFTAVCVLKEKCMDYFHVNANYIVWKTNHFTIPKEQYTI INRTASSVTFTDIASLNIQLTCNILTFGQLEQNVYGITIISGLPPEKPKNLSCIVNEGKK MRCEWDGGRETHLETNFTLKSEWATHKFADCKAKRDTPTSCTVDYSTVYFVNIEVWVEAE NALGKVTSDHINFDPVYKVKPNPPHNLSVINSEELSSILKLTWTNPSIKSVIILKYNIQY RTKDASTWSQIPPEDTASTRSSFTVQDLKPFTEYVFRIRCMKEDGKGYWSDWSEEASGIT YEDRPSKAPSFWYKIDPSHTQGYRTVQLVWKTLPPFEANGKILDYEVTLTRWKSHLQNYT VNATKLTVNLTNDRYLATLTVRNLVGKSDAAVLTIPACDFQATHPVMDLKAFPKDNMLWV EWTTPRESVKKYILEWCVLSDKAPCITDWQQEDGTVHRTYLRGNLAESKCYLITVTPVYA DGPGSPESIKAYLKQAPPSKGPTVRTKKVGKNEAVLEWDQLPVDVQNGFIRNYTIFYRTI IGNETAVNVDSSHTEYTLSSLTSDTLYMVRMAAYTDEGGKDGPEFTFTTPK
>8DPT_2 Interleukin-11 (chains B, E) GSPDPRAELDSTVLLTRSLLADTRQLAAQLRDKFPADGDHNLDSLPTLAMSAGALGALQL PGVLTRLRADLLSYLRHVQWLRRAGGSSLKTLEPELGTLQARLDRLLRRLQLLMSRLALP QPPPDPPAPPLAPPSSAWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL
>8DPT_3 Interleukin-11 receptor subunit alpha (chains C, F) GSSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVL AQADSTDEGTYICQTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLP TRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPL GASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPSQPHFLLKFRLQYR PAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGT
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant. Metcalfe, R.D., Hanssen, E., Fung, K.Y. et al. Nat Commun (2023) 14:7543-7543. DOI 10.1038/s41467-023-42754-w · PubMed
Other PDB entries of the same protein (UniProt P40189 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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