8IK3: Stimulator of interferon genes/ligand complex
Structure of Stimulator of interferon genes/ligand complex. Determined by electron microscopy at 3.3 Å resolution. Released 17 May 2023.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 20,938
- Mol. weight
- 467.92 kDa
- Ligands
- 1SY
- Released
- 17 May 2023
Explore 8IK3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8IK3 contains 137 α-helices and 70 β-strands across 8 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: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 18-34 | 17 | |
| α-helix | 40-69 | 30 | |
| α-helix | 70-72 | 3 | |
| α-helix | 73-76 | 4 | |
| α-helix | 81-88 | 8 | |
| α-helix | 92-108 | 17 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-151 | 11 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 175-185 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 1 |
| β-strand | 219-224 | 6 | 2 |
| β-strand | 228-232 | 5 | 3 |
| β-strand | 235-240 | 6 | 3 |
| β-strand | 243-249 | 7 | 2 |
| β-strand | 252-257 | 6 | 2 |
| β-strand | 259-260 | 2 | 1 |
| α-helix | 263-270 | 8 | |
| β-strand | 274 | 1 | 4 |
| α-helix | 282-300 | 19 | |
| β-strand | 309-314 | 6 | 1 |
| α-helix | 325-336 | 12 | |
Chain B: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 17-35 | 19 | |
| α-helix | 40-69 | 30 | |
| α-helix | 73-76 | 4 | |
| α-helix | 81-88 | 8 | |
| α-helix | 92-106 | 15 | |
| α-helix | 118-134 | 17 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 175-181 | 7 | |
| α-helix | 182-186 | 5 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 5 |
| β-strand | 219-224 | 6 | 6 |
| β-strand | 228-232 | 5 | 7 |
| β-strand | 235-240 | 6 | 7 |
| β-strand | 243-249 | 7 | 6 |
| β-strand | 252-257 | 6 | 6 |
| β-strand | 259-260 | 2 | 5 |
| α-helix | 263-271 | 9 | |
| β-strand | 274 | 1 | 8 |
| α-helix | 283-300 | 18 | |
| β-strand | 309-314 | 6 | 5 |
| α-helix | 325-333 | 9 | |
Chain C: 16 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 17-35 | 19 | |
| α-helix | 40-69 | 30 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-104 | 13 | |
| α-helix | 105-107 | 3 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-151 | 11 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 175-185 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 9 |
| β-strand | 219-224 | 6 | 10 |
| β-strand | 228-232 | 5 | 11 |
| β-strand | 235-240 | 6 | 11 |
| β-strand | 243-249 | 7 | 10 |
| β-strand | 252-257 | 6 | 10 |
| β-strand | 259-260 | 2 | 9 |
| α-helix | 263-271 | 9 | |
| β-strand | 274 | 1 | 8 |
| α-helix | 282-300 | 19 | |
| β-strand | 309-314 | 6 | 9 |
| α-helix | 325-334 | 10 | |
Chain D: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 18-35 | 18 | |
| α-helix | 40-69 | 30 | |
| α-helix | 73-76 | 4 | |
| α-helix | 81-88 | 8 | |
| α-helix | 94-108 | 15 | |
| α-helix | 117-134 | 18 | |
| α-helix | 141-150 | 10 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 173-175 | 3 | |
| α-helix | 176-181 | 6 | |
| α-helix | 182-186 | 5 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 12 |
| β-strand | 220-224 | 5 | 13 |
| β-strand | 228-232 | 5 | 14 |
| β-strand | 235-240 | 6 | 14 |
| β-strand | 243-249 | 7 | 13 |
| β-strand | 252-257 | 6 | 13 |
| β-strand | 259-260 | 2 | 12 |
| α-helix | 263-271 | 9 | |
| β-strand | 274 | 1 | 15 |
| α-helix | 283-300 | 18 | |
| β-strand | 309-314 | 6 | 12 |
| α-helix | 325-334 | 10 | |
Chain E: 18 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 17-35 | 19 | |
| α-helix | 40-69 | 30 | |
| α-helix | 70-72 | 3 | |
| α-helix | 82-89 | 8 | |
| α-helix | 92-104 | 13 | |
| α-helix | 105-107 | 3 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-151 | 11 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 175-185 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 16 |
| β-strand | 219-224 | 6 | 17 |
| β-strand | 228-232 | 5 | 18 |
| β-strand | 235-240 | 6 | 18 |
| β-strand | 243-249 | 7 | 17 |
| β-strand | 252-257 | 6 | 17 |
| β-strand | 259-260 | 2 | 16 |
| α-helix | 263-271 | 9 | |
| β-strand | 274 | 1 | 15 |
| α-helix | 282-300 | 19 | |
| α-helix | 306-308 | 3 | |
| β-strand | 309-314 | 6 | 16 |
| α-helix | 325-334 | 10 | |
Chain F: 18 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 17-35 | 19 | |
| α-helix | 40-69 | 30 | |
| α-helix | 70-72 | 3 | |
| α-helix | 81-88 | 8 | |
| α-helix | 92-104 | 13 | |
| α-helix | 105-107 | 3 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-151 | 11 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 175-185 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 22 |
| β-strand | 219-224 | 6 | 23 |
| β-strand | 228-232 | 5 | 24 |
| β-strand | 235-240 | 6 | 24 |
| β-strand | 243-249 | 7 | 23 |
| β-strand | 252-257 | 6 | 23 |
| β-strand | 259-260 | 2 | 22 |
| α-helix | 263-273 | 11 | |
| α-helix | 282-300 | 19 | |
| α-helix | 306-308 | 3 | |
| β-strand | 309-314 | 6 | 22 |
| α-helix | 325-334 | 10 | |
Chain G: 17 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 18-35 | 18 | |
| α-helix | 40-69 | 30 | |
| α-helix | 70-72 | 3 | |
| α-helix | 73-76 | 4 | |
| α-helix | 81-86 | 6 | |
| α-helix | 94-108 | 15 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-150 | 10 | |
| α-helix | 156-163 | 8 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 175-185 | 11 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 19 |
| β-strand | 220-224 | 5 | 20 |
| β-strand | 228-232 | 5 | 21 |
| β-strand | 235-240 | 6 | 21 |
| β-strand | 243-249 | 7 | 20 |
| β-strand | 252-257 | 6 | 20 |
| β-strand | 259-260 | 2 | 19 |
| α-helix | 263-271 | 9 | |
| α-helix | 283-300 | 18 | |
| β-strand | 309-314 | 6 | 19 |
| α-helix | 325-334 | 10 | |
Chain H: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-14 | 4 | |
| α-helix | 18-35 | 18 | |
| α-helix | 40-69 | 30 | |
| α-helix | 70-72 | 3 | |
| α-helix | 73-76 | 4 | |
| α-helix | 81-88 | 8 | |
| α-helix | 94-108 | 15 | |
| α-helix | 118-134 | 17 | |
| α-helix | 141-150 | 10 | |
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 176-185 | 10 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 25 |
| β-strand | 220-224 | 5 | 26 |
| β-strand | 228-232 | 5 | 27 |
| β-strand | 235-240 | 6 | 27 |
| β-strand | 243-249 | 7 | 26 |
| β-strand | 252-257 | 6 | 26 |
| β-strand | 259-260 | 2 | 25 |
| α-helix | 263-271 | 9 | |
| β-strand | 274 | 1 | 4 |
| α-helix | 283-301 | 19 | |
| β-strand | 309-314 | 6 | 25 |
| α-helix | 325-334 | 10 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Stimulator of interferon genes protein,Immune protein Tsi3 | A, B, C, D, E, F, G, H | protein | 521 | Homo sapiens | Q86WV6 (AlphaFold model), Q9HYC4 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>8IK3_1 Stimulator of interferon genes protein,Immune protein Tsi3 (chains A, B, C, D, E, F, G, H)
MPHSSLHPSIPCPRGHGAQKAALVLLSACLVTLWGLGEPPEHTLRYLVLHLASLQLGLLL
NGVCSLAEELRHIHSRYRGSYWRTVRACLGCPLRRGALLLLSIYFYYSLPNAVGPPFTWM
LALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIR
TYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDRAGIKDRVY
SNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILA
DAPESQNNCRLIAYQEPADDSSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQE
PELLISGMEKPLPLRTDFSLEVLFQGPVDFDKTLTHPNGLVVERPVGFDARRSAEGFRFD
EGGKLRNPRQLEVQRQDAPPPPDLASRRLGDGEARYKVEEDDGGSAGSEYRLWAAKPAGA
RWIVVSASEQSEDGEPTFALAWALLERARLQSSHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 1SY | cGAMP | C20 H24 N10 O13 P2 | 4 |
Primary citation
The mechanism of STING autoinhibition and activation. Liu, S., Yang, B., Hou, Y. et al. Mol Cell (2023) 83:1502-1518.e10. DOI 10.1016/j.molcel.2023.03.029 · PubMed
Other PDB entries of the same protein (UniProt Q86WV6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6MX3 1.36 Å, Crystal structure of human STING (G230A, H232R, R293Q) in complex with Compound 1
- 4EMT 1.5 Å, Crystal Structure of human STING bound to c-di-GMP
- 6UKZ 1.52 Å, STING C-terminal Domain Complexed with Non-cyclic Dinucleotide Compound 6
- 9CUD 1.53 Å, Human STING G230A/R293Q variant bound to diABZI-i
- 6UKU 1.68 Å, STING C-terminal Domain Complexed with Non-cyclic Dinucleotide Compound 3
- 7ZKU 1.7 Å, Crystal structure of human STING in complex with 3',3'-c-(2'F,2'dAMP-2'd<carba>GMP)
- 8STI 1.72 Å, human STING with agonist XMT-1616
- 6MX0 1.73 Å, Crystal structure of human STING apoprotein (G230A, H232R, R293Q)
- 6UKM 1.74 Å, STING C-terminal Domain Complexed with Non-cyclic Dinucleotide Compound MSA-2
- 9VZG 1.74 Å, Harnessing Noncovalent Dimerization Enables an Orally Active STING Agonist for…
- 6UL0 1.76 Å, STING C-terminal Domain Complexed with Non-cyclic Dinucleotide Compound 4
- 6XNP 1.77 Å, Crystal Structure of Human STING CTD complex with SR-717
Browse structure collections
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