MolNFT v1 · #5858 · protein
AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit alpha (P25108)
P25108: “AlphaFold monomer V2.0 prediction for acetylcholine receptor subunit alpha (P25108)”. 3 pockets (best druggability 0.45). MolNFT v1 #5858 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P25108
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x02928767Cd38aeb0E96b8eac0D163d47785dC64E
- Molecule
- Acetylcholine receptor subunit alpha
- UniProt
- P25108
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylcholine receptor subunit alpha | protein | 457 | 43% helix, 23% strand | P25108 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.45 | 0.75 | 27 | empty |
| 2 | 51 | 0.36 | 0.79 | 14 | empty |
| 3 | 50 | 0.28 | 0.75 | 10 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P25108
- Elsewhere: UniProt P25108 · AlphaFold DB P25108
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