Crystal structure of human STING apoprotein (G230A, H232R, R293Q). Determined by X-ray diffraction at 1.73 Å resolution. Released 19 Dec 2018.
Explore 6MX0 in 3D Show helices and sheets RCSB PDB PDBe
6MX0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-181 | 13 | |
| α-helix | 182-186 | 5 | |
| α-helix | 193-195 | 3 | |
| β-strand | 198-203 | 6 | 1 |
| β-strand | 219-224 | 6 | 1 |
| α-helix | 225-226 | 2 | |
| β-strand | 243-249 | 7 | 1 |
| β-strand | 252-261 | 10 | 1 |
| α-helix | 264-272 | 9 | |
| α-helix | 275-277 | 3 | |
| α-helix | 281-301 | 21 | |
| β-strand | 309-314 | 6 | 1 |
| α-helix | 325-336 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 155-163 | 9 | |
| α-helix | 164-168 | 5 | |
| α-helix | 169-181 | 13 | |
| α-helix | 182-186 | 5 | |
| α-helix | 192-195 | 4 | |
| β-strand | 198-203 | 6 | 2 |
| α-helix | 213-215 | 3 | |
| β-strand | 219-225 | 7 | 2 |
| α-helix | 226 | 1 | |
| β-strand | 242-249 | 8 | 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 | 320-322 | 3 | |
| α-helix | 325-335 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Stimulator of interferon genes protein | A, B | protein | 188 | Homo sapiens | Q86WV6 (AlphaFold model) |
>6MX0_1 Stimulator of interferon genes protein (chains A, B) SVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLS MADPNIRFLDKLPQQTADRAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQ YSQAGFSREDRLEQAKLFCQTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHL RQEEKEEV
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Discovery of a Novel cGAMP Competitive Ligand of the Inactive Form of STING. Siu, T., Altman, M.D., Baltus, G.A. et al. ACS Med Chem Lett (2019) 10:92-97. DOI 10.1021/acsmedchemlett.8b00466 · PubMed
Other PDB entries of the same protein (UniProt Q86WV6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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