Research workbench
AlphaFold monomer V2.0 prediction for flagellar L-ring protein (Q1BSV1)
Analyse AlphaFold monomer V2.0 prediction for flagellar L-ring protein (Q1BSV1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1BSV1
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6D71747Ba3BA61acAd0bA28226C08437a119C1D7
- Molecule
- Flagellar L-ring protein
- UniProt
- Q1BSV1
Structure
1 distinct chain · 17% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar L-ring protein | protein | 229 | 17% helix, 42% strand | Q1BSV1 |
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 Q1BSV1
- Elsewhere: UniProt Q1BSV1 · AlphaFold DB Q1BSV1
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