Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 158 (A2VDX9)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 158 (A2VDX9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2VDX9
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Transmembrane protein 158
- UniProt
- A2VDX9
- Pockets
- 2 · best druggability 0.43
Structure
1 distinct chain · 23% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 158 | protein | 291 | 23% helix, 15% strand | A2VDX9 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.43 | 0.75 | 21 | empty |
| 2 | 56 | 0.31 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 A2VDX9
- Elsewhere: UniProt A2VDX9 · AlphaFold DB A2VDX9
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