Research workbench
AlphaFold monomer V2.0 prediction for voltage-dependent anion- selective channel protein 1 (Q9Z2L0)
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
- Q9Z2L0
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Voltage-dependent anion-selective channel protein 1
- UniProt
- Q9Z2L0
- Pockets
- 4 · best druggability 0.49
Structure
1 distinct chain · 6% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-dependent anion-selective channel protein 1 | protein | 283 | 6% helix, 65% strand | Q9Z2L0 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.49 | 0.75 | 38 | empty |
| 2 | 150 | 0.47 | 0.77 | 27 | empty |
| 3 | 91 | 0.38 | 0.76 | 20 | empty |
| 4 | 58 | 0.34 | 0.78 | 13 | 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 Q9Z2L0
- Elsewhere: UniProt Q9Z2L0 · AlphaFold DB Q9Z2L0
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