Research workbench
AlphaFold monomer V2.0 prediction for flagellin fljm (O52529)
Analyse AlphaFold monomer V2.0 prediction for flagellin fljm (O52529) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O52529
- Type
- protein
- Length
- 273 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf6386063eD65e545110f857dE595A2a4ed178391
- UniProt
- O52529
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 273 | — | O52529 |
Compared structures
- 9CEO · Caulobacter crescentus FljJM flagellar filament (asymmetrical) · an experimental structure of the same protein · chain A against S, TM-score 0.96
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 O52529
- Elsewhere: UniProt O52529 · AlphaFold DB O52529
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