Research workbench
Structure of drosophila sting in complex with 3'2'-cgamp
Analyse Structure of drosophila sting in complex with 3'2'-cgamp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MWZ
- Type
- protein
- Length
- 1,353 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sting
- Ligands
- 4UR
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sting | protein | 351 | 52% helix, 17% strand | — |
| B | Sting | protein | 352 | 51% helix, 16% strand | — |
| C | Sting | protein | 349 | 51% helix, 17% strand | — |
| D | Sting | protein | 301 | 44% helix, 19% strand | — |
Ligands and binding sites
- 4UR · 3'2'-cGAMP · ligand · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.85 | 0.96 | 39 | 4UR |
| 2 | 264 | 0.85 | 0.96 | 34 | 4UR |
| 3 | 918 | 0.80 | 0.82 | 87 | empty |
| 4 | 1131 | 0.80 | 0.81 | 96 | empty |
| 5 | 59 | 0.57 | 0.90 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2673 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 2572 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 170 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 157 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 148 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7MWZ · Structure of drosophila STING in complex with 3'2'-cGAMP · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7MWZ · PDBe 7MWZ
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