9CUD: Human STING G230A/R293Q variant

Human STING G230A/R293Q variant bound to diABZI-i. Determined by X-ray diffraction at 1.53 Å resolution. Released 18 Jun 2025.

Method: X-ray diffraction
Resolution: 1.53 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,926
Mol. weight: 48.95 kDa
Ligands: A1A4W
Released: 18 Jun 2025

Explore 9CUD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CUD contains 18 α-helices and 10 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: 9 helices, 5 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	1
β-strand	219-224	6	1
α-helix	225-227	3
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	325-333	9

Chain B: 9 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	155-163	9
α-helix	164-168	5
α-helix	169-183	15
β-strand	198-203	6	2
α-helix	212-214	3
β-strand	219-224	6	2
α-helix	225-227	3
β-strand	243-249	7	2
β-strand	252-261	10	2
α-helix	264-273	10
α-helix	275-277	3
α-helix	281-301	21
β-strand	309-314	6	2
α-helix	325-335	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Stimulator of interferon genes protein	A, B	protein	210	Homo sapiens	Q86WV6 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9CUD_1 Stimulator of interferon genes protein (chains A, B)
MGSSHHHHHHSSGETVRFQGHMSVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLR
GAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTADRAGIKDRVYSNSIYELLENG
QRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCQTLEDILADAPESQNNCRL
IAYQEPADDSSFSLSQEVLRHLRQEEKEEV

Ligands and cofactors

ID	Name	Formula	Copies
A1A4W	(2E)-1-[(2E)-4-{(2E)-5-carbamoyl-2-[(1-ethyl-3-methyl-1H-pyrazole-5-carbonyl)im…	C46 H52 N12 O6	1

Primary citation

Orthosteric STING inhibition elucidates molecular correction of SAVI STING. Xie, T., Ruzanov, M., Critton, D. et al. Nat Commun (2025) 16:5695-5695. DOI 10.1038/s41467-025-60632-5 · 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
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
7KW1 1.8 Å, Structure of hSTING in complex with novel carbocyclic pyrimidine CDN-3

Browse structure collections

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