8SV1: Caspase-1 complex with interleukin-18

Caspase-1 complex with interleukin-18. Determined by electron microscopy at 3.5 Å resolution. Released 8 May 2024.

Method
Electron microscopy
Resolution
3.5 Å
Organism
Homo sapiens
Chains
6
Atoms
6,330
Mol. weight
97.43 kDa
Released
8 May 2024

Explore 8SV1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain a: 5 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand152111
β-strand164-169612
α-helix182-19615
β-strand199-204612
α-helix208-21912
α-helix224-2263
β-strand230-235612
β-strand238113
β-strand242-244313
β-strand255-257313
α-helix258-2636
α-helix271-2733
β-strand279-283512
β-strand292-29435
Chain A: 5 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand15211
β-strand165-16952
α-helix182-19615
β-strand200-20452
α-helix208-22013
α-helix222-2265
β-strand231-23552
β-strand238-23923
β-strand242-24433
β-strand255-25623
α-helix258-2647
α-helix271-2733
β-strand278-28362
β-strand295-29624
Chain b: 2 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand318-31924
β-strand328112
β-strand331114
β-strand340-341215
β-strand342116
β-strand346116
α-helix348-36013
α-helix366-37510
β-strand388114
β-strand389110
β-strand39219
β-strand397111
Chain B: 2 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand320-32235
β-strand327-32822
β-strand33116
β-strand340-34127
β-strand34218
β-strand34618
α-helix348-36013
α-helix366-37510
β-strand38816
β-strand38919
β-strand392110
β-strand39711
Chains c and C: 2 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand18120
β-strand23120
β-strand24-25221
α-helix331
β-strand34-35215
β-strand45-46221
β-strand84-88522
β-strand97-102622
β-strand108-111422
β-strand118-121422
β-strand137-141522
β-strand148-153622
β-strand161-166621
β-strand169-174621
β-strand185-187321
β-strand188-190322
α-helix191-1922

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Caspase-1A, aprotein148Homo sapiensP29466 (AlphaFold model)
Caspase-1B, bprotein88Homo sapiensP29466 (AlphaFold model)
Interleukin-18C, cprotein188Homo sapiensQ14116 (AlphaFold model)
Sequence of entity 1 (A, a), FASTA
>8SV1_1 Caspase-1 (chains A, a)
AEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTAS
DMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKN
CPSLKDKPKVIIIQACRGDSPGVVWFKD
Sequence of entity 2 (B, b), FASTA
>8SV1_2 Caspase-1 (chains B, b)
AIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFS
FEQPDGRAQMPTTERVTLTRCFYLFPGH
Sequence of entity 3 (C, c), FASTA
>8SV1_3 Interleukin-18 (chains C, c)
VEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPL
FEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPP
DNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSI
MFTVQNED

Primary citation

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:

Browse structure collections

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