Research workbench
AlphaFold monomer V2.0 prediction for F-actin-capping protein subunit alpha-2 (Q2IBB9)
Analyse AlphaFold monomer V2.0 prediction for F-actin-capping protein subunit alpha-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2IBB9
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0787bC904B7be1a8Bd84a0CF1b68B9B4567D88eb
- Molecule
- F-actin-capping protein subunit alpha-2
- UniProt
- Q2IBB9
- Pockets
- 2 · best druggability 0.43
Structure
1 distinct chain · 38% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F-actin-capping protein subunit alpha-2 | protein | 286 | 38% helix, 31% strand | Q2IBB9 |
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 | 153 | 0.43 | 0.75 | 22 | empty |
| 2 | 57 | 0.30 | 0.75 | 15 | 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 Q2IBB9
- Elsewhere: UniProt Q2IBB9 · AlphaFold DB Q2IBB9
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