Research workbench
Crystal structure of anemone sting (nematostella vectensis) in apo 'unrotated' closed conformation
Analyse Crystal structure of anemone sting (nematostella vectensis) in apo 'unrotated'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CFR
- Type
- protein
- Length
- 344 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stimulator of interferon genes
- UniProt
- A7SLZ2
- Ligands
- CA
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Stimulator of interferon genes | protein | 172 | 38% helix, 23% strand | A7SLZ2 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.84 | 0.94 | 42 | empty |
| 2 | 86 | 0.63 | 0.90 | 21 | empty |
| 3 | 139 | 0.47 | 0.77 | 29 | empty |
| 4 | 75 | 0.45 | 0.81 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1981 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 5CFR · Crystal structure of anemone STING (Nematostella vectensis) in apo 'unrotated' closed… · the same entry in another collection · chain A against A, TM-score 1.00
- A7SLZ2 · AlphaFold monomer V2.0 prediction for stimulator of interferon genes protein (A7SLZ2) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 A7SLZ2
- Elsewhere: RCSB PDB 5CFR · PDBe 5CFR · UniProt A7SLZ2
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