8IK0: Stimulator of interferon genes

Cryo-EM structure of Stimulator of interferon genes. Determined by electron microscopy at 3.3 Å resolution. Released 17 May 2023.

Method: Electron microscopy
Resolution: 3.3 Å
Organisms: Gallus gallus, Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Chains: 8
Atoms: 19,536
Mol. weight: 442.26 kDa
Released: 17 May 2023

Explore 8IK0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8IK0 contains 145 α-helices and 62 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: 20 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	24-40	17
α-helix	47-59	13
α-helix	60-62	3
α-helix	63-75	13
α-helix	79-82	4
α-helix	88-93	6
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	161-168	8
α-helix	169-173	5
α-helix	174-176	3
α-helix	178-180	3
α-helix	181-190	10
α-helix	192-196	5
β-strand	203-208	6	1
α-helix	217-220	4
β-strand	224-229	6	1
α-helix	230-232	3
β-strand	233-237	5	2
β-strand	241-246	6	2
β-strand	248-253	6	1
β-strand	259-266	8	1
α-helix	268-277	10
α-helix	287-304	18
β-strand	314-319	6	1
α-helix	329-341	13

Chain B: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	18-20	3
α-helix	24-40	17
α-helix	49-78	30
α-helix	79-83	5
α-helix	88-94	7
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	160-168	9
α-helix	169-173	5
α-helix	178-180	3
α-helix	181-190	10
α-helix	192-195	4
β-strand	203-208	6	3
α-helix	217-220	4
β-strand	224-228	5	4
β-strand	232-237	6	2
β-strand	240-241	2	2
α-helix	242-244	3
β-strand	249-253	5	4
β-strand	259-263	5	4
β-strand	264-266	3	3
α-helix	268-278	11
α-helix	286-305	20
β-strand	314-319	6	3
α-helix	329-341	13

Chain C: 18 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	24-40	17
α-helix	47-59	13
α-helix	63-75	13
α-helix	79-83	5
α-helix	88-93	6
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	161-168	8
α-helix	169-173	5
α-helix	174-176	3
α-helix	181-188	8
α-helix	192-196	5
β-strand	203-206	4	5
α-helix	217-220	4
β-strand	224-229	6	5
α-helix	230-232	3
β-strand	233-237	5	6
β-strand	241-246	6	6
β-strand	248-253	6	5
β-strand	259-266	8	5
α-helix	268-277	10
α-helix	287-305	19
β-strand	314-317	4	5
α-helix	329-339	11

Chain D: 20 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	24-40	17
α-helix	47-59	13
α-helix	60-62	3
α-helix	63-75	13
α-helix	79-82	4
α-helix	88-93	6
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	161-168	8
α-helix	169-173	5
α-helix	174-176	3
α-helix	178-180	3
α-helix	181-190	10
α-helix	192-196	5
β-strand	203-208	6	9
α-helix	217-220	4
β-strand	224-229	6	9
α-helix	230-232	3
β-strand	233-237	5	10
β-strand	241-246	6	10
β-strand	248-253	6	9
β-strand	259-266	8	9
α-helix	268-277	10
α-helix	287-305	19
β-strand	314-319	6	9
α-helix	329-341	13

Chain E: 18 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	24-40	17
α-helix	47-59	13
α-helix	63-75	13
α-helix	79-83	5
α-helix	88-94	7
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	161-168	8
α-helix	169-173	5
α-helix	174-176	3
α-helix	181-188	8
α-helix	192-196	5
β-strand	203-208	6	13
α-helix	217-220	4
β-strand	224-229	6	13
α-helix	230-232	3
β-strand	233-237	5	14
β-strand	241-246	6	14
β-strand	248-253	6	13
β-strand	259-266	8	13
α-helix	268-277	10
α-helix	287-305	19
β-strand	314-319	6	13
α-helix	329-341	13

Chain F: 17 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	18-20	3
α-helix	24-40	17
α-helix	47-75	29
α-helix	79-83	5
α-helix	88-94	7
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	160-168	9
α-helix	169-173	5
α-helix	181-190	10
α-helix	192-195	4
β-strand	203-208	6	7
α-helix	217-220	4
β-strand	224-228	5	8
β-strand	232-237	6	6
β-strand	240-241	2	6
α-helix	242-244	3
β-strand	249-253	5	8
β-strand	259-263	5	8
β-strand	264-266	3	7
α-helix	268-278	11
α-helix	286-305	20
β-strand	314-319	6	7
α-helix	330-341	12

Chain G: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	18-20	3
α-helix	24-40	17
α-helix	49-75	27
α-helix	79-83	5
α-helix	88-94	7
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	160-168	9
α-helix	169-173	5
α-helix	178-180	3
α-helix	181-190	10
α-helix	192-195	4
β-strand	203-208	6	11
α-helix	217-220	4
β-strand	224-228	5	12
β-strand	232-237	6	10
β-strand	240-241	2	10
α-helix	242-244	3
β-strand	249-253	5	12
β-strand	259-263	5	12
β-strand	264-266	3	11
α-helix	268-278	11
α-helix	286-305	20
β-strand	314-319	6	11
α-helix	329-341	13

Chain H: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	18-20	3
α-helix	24-40	17
α-helix	47-75	29
α-helix	79-83	5
α-helix	88-94	7
α-helix	100-112	13
α-helix	124-139	16
α-helix	146-155	10
α-helix	160-168	9
α-helix	169-173	5
α-helix	181-190	10
α-helix	192-196	5
β-strand	203-208	6	15
β-strand	224-228	5	16
β-strand	233-237	5	14
β-strand	240-241	2	14
α-helix	242-244	3
β-strand	249-253	5	16
β-strand	256	1	17
β-strand	258	1	17
β-strand	259-263	5	16
β-strand	264-266	3	15
α-helix	268-278	11
α-helix	286-305	20
β-strand	314-319	6	15
α-helix	330-341	12

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	490	Gallus gallus, Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)	E1C7U0 (AlphaFold model), Q9HYC4 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>8IK0_1 Stimulator of interferon genes protein,Immune protein Tsi3 (chains A, B, C, D, E, F, G, H)
MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPITRRVCTQLAAL
QLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWHLALLLVGGSAYLDPPEDNGH
SPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRL
KECMEEISRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGI
KRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSL
RDILGSSKECAGLYRLIAYEEPAEPESHFLSGLILWHLQQQQREEYMVLEVLFQGPVDFD
KTLTHPNGLVVERPVGFDARRSAEGFRFDEGGKLRNPRQLEVQRQDAPPPPDLASRRLGD
GEARYKVEEDDGGSAGSEYRLWAAKPAGARWIVVSASEQSEDGEPTFALAWALLERARLQ
SSHHHHHHHH

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 E1C7U0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6NT9 3.3 Å, Cryo-EM structure of the complex between human TBK1 and chicken STING
6NT6 4.0 Å, Cryo-EM structure of full-length chicken STING in the apo state
6NT7 4.0 Å, Cryo-EM structure of full-length chicken STING in the cGAMP-bound dimeric state
6NT8 6.5 Å, Cryo-EM structure of full-length chicken STING in the cGAMP-bound tetrameric state

Browse structure collections

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