Research workbench
AlphaFold monomer V2.0 prediction for phase 2 flagellin (P52616)
Analyse AlphaFold monomer V2.0 prediction for phase 2 flagellin (P52616) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P52616
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3d6707a69900E10a2dEC242C7C8B483353cebf36
- UniProt
- P52616
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 506 | — | P52616 |
Compared structures
- 5YUD · Flagellin derivative in complex with the nlr protein NAIP5 · an experimental structure of the same protein · chain A against C, TM-score 0.11
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 P52616
- Elsewhere: UniProt P52616 · AlphaFold DB P52616
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