Research workbench
AlphaFold monomer V2.0 prediction for voltage-dependent anion- selective channel protein 3 (Q5R7V4)
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
- Q5R7V4
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF9719Da6F4C39eC4094366C9bF798ab649E347b3
- Molecule
- Voltage-dependent anion-selective channel protein 3
- UniProt
- Q5R7V4
- Pockets
- 4 · best druggability 0.44
Structure
1 distinct chain · 5% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-dependent anion-selective channel protein 3 | protein | 284 | 5% helix, 64% strand | Q5R7V4 |
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 | 79 | 0.44 | 0.81 | 24 | empty |
| 2 | 153 | 0.43 | 0.75 | 30 | empty |
| 3 | 148 | 0.43 | 0.75 | 38 | empty |
| 4 | 78 | 0.32 | 0.74 | 21 | 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 Q5R7V4
- Elsewhere: UniProt Q5R7V4 · AlphaFold DB Q5R7V4
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