Research workbench
AlphaFold monomer V2.0 prediction for flagellar motor switch protein flim (P26418)
Analyse AlphaFold monomer V2.0 prediction for flagellar motor switch protein flim… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26418
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x48cAFA58220078394F6FF347a5D7047Dbd6CD9CB
- UniProt
- P26418
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 334 | — | P26418 |
Compared structures
- 8YJT · Cryo-EM structure of the flagellar C ring in the CCW state · an experimental structure of the same protein · chain A against AM, TM-score 0.64
- 8XP0 · Cryo-EM structure of the protomers of the C ring in the CCW state · an experimental structure of the same protein · chain A against O, TM-score 0.64
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 P26418
- Elsewhere: UniProt P26418 · AlphaFold DB P26418
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