Research workbench
Crystal structure of rat STING in complex with cyclic GMP-AMP with 2'5'and 3'5'phosphodiester linkage(2'3'-cGAMP)
Analyse Crystal structure of rat STING in complex with cyclic GMP-AMP with 2'5'and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GRM
- Type
- protein
- Length
- 378 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.55
- Source
- Rattus norvegicus
- Molecule
- Stimulator of interferon genes protein
- UniProt
- F1M391
- Ligands
- 1SY
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · resolution 1.55 · 2 distinct chains · 46% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stimulator of interferon genes protein | protein | 188 | 44% helix, 24% strand | F1M391 |
| B | Stimulator of interferon genes protein | protein | 190 | 48% helix, 24% strand | F1M391 |
Ligands and binding sites
- 1SY · cGAMP · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 344 | 0.81 | 0.91 | 50 | 1SY |
| 2 | 56 | 0.30 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1880 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5GRM · Crystal structure of rat sting in complex with cyclic gmp-AMP with 2'5'AND… · the same entry in another collection · chain A against A, TM-score 1.00
- F1M391 · AlphaFold monomer V2.0 prediction for stimulator of interferon genes protein (F1M391) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 F1M391
- Elsewhere: RCSB PDB 5GRM · PDBe 5GRM · UniProt F1M391
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