Research workbench
AlphaFold monomer V2.0 prediction for flagellin (P02968)
Analyse AlphaFold monomer V2.0 prediction for flagellin (P02968) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P02968
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x931f6ee42097C0611b7f12a7b3a279ef973b9cf4
- UniProt
- P02968
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 304 | — | P02968 |
Compared structures
- 5MAW · Crystal structure of the flagellin-flis complex from bacillus subtilis · an experimental structure of the same protein · chain A against D, TM-score 0.67
- 5MAW · Crystal structure of the flagellin-FliS complex from Bacillus subtilis · an experimental structure of the same protein · chain A against D, TM-score 0.67
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 P02968
- Elsewhere: UniProt P02968 · AlphaFold DB P02968
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