Research workbench
AlphaFold monomer V2.0 prediction for voltage-dependent anion- selective channel protein 2 (P86223)
Analyse AlphaFold monomer V2.0 prediction for voltage-dependent anion- selective… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P86223
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Voltage-dependent anion-selective channel protein 2
- UniProt
- P86223
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 5% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-dependent anion-selective channel protein 2 | protein | 295 | 5% helix, 63% strand | P86223 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.52 | 0.79 | 31 | empty |
| 2 | 206 | 0.48 | 0.75 | 37 | empty |
| 3 | 123 | 0.41 | 0.76 | 22 | empty |
| 4 | 94 | 0.37 | 0.75 | 24 | 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 P86223
- Elsewhere: UniProt P86223 · AlphaFold DB P86223
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