Research workbench
Structural basis of cytosolic DNA recognition by innate immune receptors
Analyse Structural basis of cytosolic DNA recognition by innate immune receptors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RLN
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-interferon-inducible protein 16
- UniProt
- Q16666
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-interferon-inducible protein 16 | protein | 189 | 11% helix, 51% strand | Q16666 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.48 | 0.77 | 34 | empty |
Compared structures
- 3RLN · Structural Basis of Cytosolic DNA Recognition by Innate Immune Receptors · the same entry in another collection · chain A against A, TM-score 1.00
- Q16666 · AlphaFold monomer V2.0 prediction for gamma-interferon-inducible protein 16 (Q16666) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q16666
- Elsewhere: RCSB PDB 3RLN · PDBe 3RLN · UniProt Q16666
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