Research workbench
AlphaFold monomer V2.0 prediction for flagellin (B7USU2)
Analyse AlphaFold monomer V2.0 prediction for flagellin (B7USU2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7USU2
- Type
- protein
- Length
- 548 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE5B7848EfB6C059c218398aB45e0496Ebc72Dc08
- UniProt
- B7USU2
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 548 | — | B7USU2 |
Compared structures
- 7SQJ · Cryo-EM structure of the seam subunits of the enteropathogenic E. COLI O127:H6 flagellar… · an experimental structure of the same protein · chain A against A, TM-score 0.55
- 7SQJ · Cryo-EM structure of the seam subunits of the enteropathogenic E. coli O127:H6 flagellar… · an experimental structure of the same protein · chain A against A, TM-score 0.55
- 8CVI · Cryo-EM structure of the supercoiled EPEC H6 flagellar filament core Curly I waveform · an experimental structure of the same protein · chain A against M, TM-score 0.48
- 8CYE · Cryo-EM asymmetric reconstruction of the EPEC H6 bacterial flagellar filament Normal… · an experimental structure of the same protein · chain A against T, TM-score 0.48
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 B7USU2
- Elsewhere: UniProt B7USU2 · AlphaFold DB B7USU2
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