Research workbench
AlphaFold monomer V2.0 prediction for aliphatic sulfonates import ATP-binding protein ssub (A1A9L0)
Analyse AlphaFold monomer V2.0 prediction for aliphatic sulfonates import ATP-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1A9L0
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Aliphatic sulfonates import ATP-binding protein ssub
- UniProt
- A1A9L0
- Pockets
- 3 · best druggability 0.40
Structure
1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aliphatic sulfonates import ATP-binding protein ssub | protein | 255 | 37% helix, 24% strand | A1A9L0 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.40 | 0.76 | 14 | empty |
| 2 | 106 | 0.40 | 0.76 | 24 | empty |
| 3 | 82 | 0.33 | 0.74 | 14 | 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 A1A9L0
- Elsewhere: UniProt A1A9L0 · AlphaFold DB A1A9L0
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