4LOI: HSTING(H232)

Crystal structure of hSTING(H232) in complex with c[G(2',5')pA(2',5')p]. Determined by X-ray diffraction at 1.89 Å resolution. Released 14 Aug 2013.

Method: X-ray diffraction
Resolution: 1.89 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,219
Mol. weight: 43.82 kDa
Ligands: 1YC, PO4
Released: 14 Aug 2013

Explore 4LOI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LOI contains 20 α-helices and 14 β-strands across 2 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: 10 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	155-163	9
α-helix	164-168	5
α-helix	169-182	14
α-helix	193-195	3
β-strand	198-203	6	1
α-helix	212-215	4
β-strand	219-224	6	1
α-helix	225-227	3
β-strand	228-232	5	2
β-strand	235-240	6	2
β-strand	243-249	7	1
β-strand	252-261	10	1
α-helix	264-273	10
α-helix	275-277	3
α-helix	281-300	20
β-strand	309-314	6	1
α-helix	325-336	12

Chain B: 10 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	155-163	9
α-helix	164-168	5
α-helix	169-185	17
α-helix	193-195	3
β-strand	198-203	6	3
α-helix	212-215	4
β-strand	219-224	6	3
α-helix	225-227	3
β-strand	228-232	5	4
β-strand	235-240	6	4
β-strand	243-249	7	3
β-strand	252-261	10	3
α-helix	264-273	10
α-helix	275-277	3
α-helix	281-301	21
β-strand	309-314	6	3
α-helix	325-335	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Stimulator of interferon genes protein	A, B	protein	188	Homo sapiens	Q86WV6 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4LOI_1 Stimulator of interferon genes protein (chains A, B)
SVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLS
MADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQ
YSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHL
RQEEKEEV

Ligands and cofactors

ID	Name	Formula	Copies
1YC	2-amino-9-[(1R,3R,6R,8R,9R,11S,14R,16R,17R,18R)-16-(6-amino-9H-purin-9-yl)-3,11…	C20 H24 N10 O13 P2	1
PO4	Phosphate ion	O4 P	1

Primary citation

Structure-Function Analysis of STING Activation by c[G(2',5')pA(3',5')p] and Targeting by Antiviral DMXAA. Gao, P., Ascano, M., Zillinger, T. et al. Cell (2013) 154:748-762. DOI 10.1016/j.cell.2013.07.023 · 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

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