Research workbench
AlphaFold monomer V2.0 prediction for flagellar L-ring protein (A0KB90)
Analyse AlphaFold monomer V2.0 prediction for flagellar L-ring protein (A0KB90) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0KB90
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Flagellar L-ring protein
- UniProt
- A0KB90
- Pockets
- 1 · best druggability 0.30
Structure
1 distinct chain · 19% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar L-ring protein | protein | 229 | 19% helix, 43% strand | A0KB90 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.30 | 0.76 | 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 A0KB90
- Elsewhere: UniProt A0KB90 · AlphaFold DB A0KB90
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