Research workbench
AlphaFold monomer V2.0 prediction for tubulin alpha-1 chain (Q6VAG1)
Analyse AlphaFold monomer V2.0 prediction for tubulin alpha-1 chain (Q6VAG1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6VAG1
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x65b42577b5Bb934B59afF2aA701E1BA18026B799
- Molecule
- Tubulin alpha-1 chain
- UniProt
- Q6VAG1
- Pockets
- 4 · best druggability 0.62
Structure
1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1 chain | protein | 451 | 46% helix, 18% strand | Q6VAG1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.62 | 0.83 | 37 | empty |
| 2 | 80 | 0.38 | 0.77 | 17 | empty |
| 3 | 80 | 0.37 | 0.77 | 18 | empty |
| 4 | 56 | 0.32 | 0.77 | 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 Q6VAG1
- Elsewhere: UniProt Q6VAG1 · AlphaFold DB Q6VAG1
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