Research workbench
AlphaFold monomer V2.0 prediction for saga-associated factor 29 (Q9DA08)
Analyse AlphaFold monomer V2.0 prediction for saga-associated factor 29 (Q9DA08) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9DA08
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- Saga-associated factor 29
- UniProt
- Q9DA08
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Saga-associated factor 29 | protein | 293 | 41% helix, 22% strand | Q9DA08 |
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 | 600 | 0.66 | 0.76 | 54 | empty |
| 2 | 135 | 0.49 | 0.79 | 24 | empty |
| 3 | 94 | 0.48 | 0.81 | 22 | empty |
| 4 | 71 | 0.31 | 0.74 | 13 | empty |
| 5 | 50 | 0.26 | 0.73 | 9 | 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 Q9DA08
- Elsewhere: UniProt Q9DA08 · AlphaFold DB Q9DA08
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