Research workbench
AlphaFold monomer V2.0 prediction for tubulin beta-1 chain (P25862)
Analyse AlphaFold monomer V2.0 prediction for tubulin beta-1 chain (P25862) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P25862
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Tubulin beta-1 chain
- UniProt
- P25862
- Pockets
- 5 · best druggability 0.68
Structure
1 distinct chain · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin beta-1 chain | protein | 386 | 53% helix, 16% strand | P25862 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 783 | 0.68 | 0.75 | 59 | empty |
| 2 | 162 | 0.49 | 0.77 | 25 | empty |
| 3 | 72 | 0.36 | 0.77 | 17 | empty |
| 4 | 84 | 0.35 | 0.76 | 17 | empty |
| 5 | 54 | 0.30 | 0.75 | 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 P25862
- Elsewhere: UniProt P25862 · AlphaFold DB P25862
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