Research workbench
Sting C-terminal domain complexed with non-cyclic dinucleotide compound msa-2
Analyse Sting C-terminal domain complexed with non-cyclic dinucleotide compound msa-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UKM
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion protein of ubiquitin-like protein SMT3 and stimulator of interferon protein…
- UniProt
- Q12306, A0A2R3XZB7
- Ligands
- QAD
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusion protein of ubiquitin-like protein SMT3 and stimulator of interferon protein C-terminal domain | protein | 176 | 46% helix, 29% strand | Q12306, A0A2R3XZB7 |
Ligands and binding sites
- QAD · 4-(5,6-dimethoxy-1-benzothiophen-2-yl)-4-oxobutanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.36 | 0.75 | 17 | empty |
| 2 | 69 | 0.31 | 0.75 | 17 | empty |
| 3 | 66 | 0.28 | 0.73 | 14 | empty |
Compared structures
- 6UKM · STING C-terminal Domain Complexed with Non-cyclic Dinucleotide Compound MSA-2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q12306 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein SMT3 (Q12306) · a predicted model of the same protein · chain A against A, TM-score 0.19
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q12306
- Every structure of UniProt A0A2R3XZB7
- Elsewhere: RCSB PDB 6UKM · PDBe 6UKM · UniProt Q12306 · UniProt A0A2R3XZB7
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