Research workbench
AlphaFold monomer V2.0 prediction for vacuolar basic amino acid transporter 3 (P25594)
Analyse AlphaFold monomer V2.0 prediction for vacuolar basic amino acid transporter 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P25594
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Vacuolar basic amino acid transporter 3
- UniProt
- P25594
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar basic amino acid transporter 3 | protein | 458 | 74% helix, 0% strand | P25594 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 460 | 0.64 | 0.76 | 39 | empty |
| 2 | 348 | 0.59 | 0.76 | 39 | empty |
| 3 | 66 | 0.43 | 0.81 | 18 | empty |
| 4 | 98 | 0.40 | 0.75 | 20 | 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 P25594
- Elsewhere: UniProt P25594 · AlphaFold DB P25594
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