Research workbench
AlphaFold monomer V2.0 prediction for voltage-dependent anion- selective channel protein 2 (P81155)
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
- P81155
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x064FA49c6b8dFe284029F65208DDf88b7F02240e
- Molecule
- Voltage-dependent anion-selective channel protein 2
- UniProt
- P81155
- Pockets
- 6 · best druggability 0.46
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 | P81155 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.46 | 0.78 | 17 | empty |
| 2 | 137 | 0.44 | 0.77 | 26 | empty |
| 3 | 122 | 0.41 | 0.76 | 22 | empty |
| 4 | 118 | 0.40 | 0.75 | 32 | empty |
| 5 | 71 | 0.32 | 0.75 | 16 | 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 P81155
- Elsewhere: UniProt P81155 · AlphaFold DB P81155
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