4EMT: Human STING

Crystal Structure of human STING bound to c-di-GMP. Determined by X-ray diffraction at 1.5 Å resolution. Released 13 Jun 2012.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,155
Mol. weight: 43.97 kDa
Ligands: CA, C2E
Released: 13 Jun 2012

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

Secondary structure: helices and β-sheets

4EMT contains 22 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: 10 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	156-163	8
α-helix	164-168	5
α-helix	169-185	17
α-helix	193-195	3
β-strand	198-203	6	1
α-helix	212-215	4
β-strand	219-225	7	1
β-strand	242-249	8	1
β-strand	252-261	10	1
α-helix	264-272	9
α-helix	275-277	3
α-helix	281-301	21
α-helix	303-306	4
β-strand	309-314	6	1
α-helix	325-333	9

Chain B: 12 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	191-195	5
β-strand	198-203	6	2
α-helix	212-215	4
β-strand	219-224	6	2
α-helix	225-226	2
β-strand	243-249	7	2
β-strand	252-261	10	2
α-helix	264-273	10
α-helix	275-277	3
α-helix	281-300	20
α-helix	303-307	5
β-strand	309-314	6	2
α-helix	320-322	3
α-helix	325-335	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transmembrane protein 173	A, B	protein	188	Homo sapiens	Q86WV6 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4EMT_1 Transmembrane protein 173 (chains A, B)
SVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLS
MADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQ
YSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHL
RQEEKEEV

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
C2E	9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxi…	C20 H24 N10 O14 P2	1

Primary citation

Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Shu, C., Yi, G., Watts, T. et al. Nat Struct Mol Biol (2012) 19:722-724. DOI 10.1038/nsmb.2331 · 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
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
7KW1 1.8 Å, Structure of hSTING in complex with novel carbocyclic pyrimidine CDN-3

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