Research workbench
AlphaFold monomer V2.0 prediction for phagocyte signaling-impaired protein (Q294E0)
Analyse AlphaFold monomer V2.0 prediction for phagocyte signaling-impaired protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q294E0
- Type
- protein
- Length
- 962 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2b47CE81494c5321B3929F4cE4EA361c06Eba2E2
- Molecule
- Phagocyte signaling-impaired protein
- UniProt
- Q294E0
- Pockets
- 12 · best druggability 0.71
Structure
1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phagocyte signaling-impaired protein | protein | 962 | 72% helix, 0% strand | Q294E0 |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.71 | 0.98 | 19 | empty |
| 2 | 268 | 0.62 | 0.80 | 28 | empty |
| 3 | 225 | 0.57 | 0.78 | 22 | empty |
| 4 | 187 | 0.48 | 0.76 | 22 | empty |
| 5 | 118 | 0.48 | 0.79 | 22 | empty |
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 Q294E0
- Elsewhere: UniProt Q294E0 · AlphaFold DB Q294E0
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