Caspase-1 complex with interleukin-18. Determined by electron microscopy at 3.5 Å resolution. Released 8 May 2024.
Explore 8SV1 in 3D Show helices and sheets RCSB PDB PDBe
8SV1 contains 18 α-helices and 68 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 | 152 | 1 | 11 |
| β-strand | 164-169 | 6 | 12 |
| α-helix | 182-196 | 15 | |
| β-strand | 199-204 | 6 | 12 |
| α-helix | 208-219 | 12 | |
| α-helix | 224-226 | 3 | |
| β-strand | 230-235 | 6 | 12 |
| β-strand | 238 | 1 | 13 |
| β-strand | 242-244 | 3 | 13 |
| β-strand | 255-257 | 3 | 13 |
| α-helix | 258-263 | 6 | |
| α-helix | 271-273 | 3 | |
| β-strand | 279-283 | 5 | 12 |
| β-strand | 292-294 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 152 | 1 | 1 |
| β-strand | 165-169 | 5 | 2 |
| α-helix | 182-196 | 15 | |
| β-strand | 200-204 | 5 | 2 |
| α-helix | 208-220 | 13 | |
| α-helix | 222-226 | 5 | |
| β-strand | 231-235 | 5 | 2 |
| β-strand | 238-239 | 2 | 3 |
| β-strand | 242-244 | 3 | 3 |
| β-strand | 255-256 | 2 | 3 |
| α-helix | 258-264 | 7 | |
| α-helix | 271-273 | 3 | |
| β-strand | 278-283 | 6 | 2 |
| β-strand | 295-296 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 318-319 | 2 | 4 |
| β-strand | 328 | 1 | 12 |
| β-strand | 331 | 1 | 14 |
| β-strand | 340-341 | 2 | 15 |
| β-strand | 342 | 1 | 16 |
| β-strand | 346 | 1 | 16 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-375 | 10 | |
| β-strand | 388 | 1 | 14 |
| β-strand | 389 | 1 | 10 |
| β-strand | 392 | 1 | 9 |
| β-strand | 397 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 320-322 | 3 | 5 |
| β-strand | 327-328 | 2 | 2 |
| β-strand | 331 | 1 | 6 |
| β-strand | 340-341 | 2 | 7 |
| β-strand | 342 | 1 | 8 |
| β-strand | 346 | 1 | 8 |
| α-helix | 348-360 | 13 | |
| α-helix | 366-375 | 10 | |
| β-strand | 388 | 1 | 6 |
| β-strand | 389 | 1 | 9 |
| β-strand | 392 | 1 | 10 |
| β-strand | 397 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18 | 1 | 20 |
| β-strand | 23 | 1 | 20 |
| β-strand | 24-25 | 2 | 21 |
| α-helix | 33 | 1 | |
| β-strand | 34-35 | 2 | 15 |
| β-strand | 45-46 | 2 | 21 |
| β-strand | 84-88 | 5 | 22 |
| β-strand | 97-102 | 6 | 22 |
| β-strand | 108-111 | 4 | 22 |
| β-strand | 118-121 | 4 | 22 |
| β-strand | 137-141 | 5 | 22 |
| β-strand | 148-153 | 6 | 22 |
| β-strand | 161-166 | 6 | 21 |
| β-strand | 169-174 | 6 | 21 |
| β-strand | 185-187 | 3 | 21 |
| β-strand | 188-190 | 3 | 22 |
| α-helix | 191-192 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Caspase-1 | A, a | protein | 148 | Homo sapiens | P29466 (AlphaFold model) |
| Caspase-1 | B, b | protein | 88 | Homo sapiens | P29466 (AlphaFold model) |
| Interleukin-18 | C, c | protein | 188 | Homo sapiens | Q14116 (AlphaFold model) |
>8SV1_1 Caspase-1 (chains A, a) AEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTAS DMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKN CPSLKDKPKVIIIQACRGDSPGVVWFKD
>8SV1_2 Caspase-1 (chains B, b) AIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFS FEQPDGRAQMPTTERVTLTRCFYLFPGH
>8SV1_3 Interleukin-18 (chains C, c) VEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPL FEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPP DNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSI MFTVQNED
Structural transitions enable interleukin-18 maturation and signaling. Dong, Y., Bonin, J.P., Devant, P. et al. Immunity (2024) 57:1533-1548.e10. DOI 10.1016/j.immuni.2024.04.015 · PubMed
Other PDB entries of the same protein (UniProt P29466 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8SV1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.