Research workbench
AlphaFold monomer V2.0 prediction for follistatin (A5YT95)
Analyse AlphaFold monomer V2.0 prediction for follistatin (A5YT95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5YT95
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Follistatin
- UniProt
- A5YT95
- Pockets
- 2 · best druggability 0.46
Structure
1 distinct chain · 19% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Follistatin | protein | 344 | 19% helix, 24% strand | A5YT95 |
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 | 79 | 0.46 | 0.82 | 16 | empty |
| 2 | 113 | 0.38 | 0.74 | 21 | empty |
Modifications
Observed in the structure: 18 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 A5YT95
- Elsewhere: UniProt A5YT95 · AlphaFold DB A5YT95
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