Research workbench
AlphaFold monomer V2.0 prediction for aliphatic sulfonates import ATP-binding protein ssub (P0AAI1)
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
- P0AAI1
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Aliphatic sulfonates import ATP-binding protein ssub
- UniProt
- P0AAI1
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aliphatic sulfonates import ATP-binding protein ssub | protein | 255 | 38% helix, 24% strand | P0AAI1 |
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 | 104 | 0.42 | 0.77 | 17 | empty |
| 2 | 63 | 0.42 | 0.81 | 12 | empty |
| 3 | 86 | 0.34 | 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 P0AAI1
- Elsewhere: UniProt P0AAI1 · AlphaFold DB P0AAI1
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