Research workbench
AlphaFold monomer V2.0 prediction for flagella basal body P-ring formation protein flga (P40131)
Analyse AlphaFold monomer V2.0 prediction for flagella basal body P-ring formation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P40131
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- UniProt
- P40131
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 219 | — | P40131 |
Compared structures
- 3VKI · Monoclinic Crystal Structure of Salmonella FlgA in closed form · an experimental structure of the same protein · chain A against B, TM-score 0.88
- 3VKI · Monoclinic crystal structure of salmonella flga in closed form · an experimental structure of the same protein · chain A against B, TM-score 0.88
- 3VJP · Orthorhombic Crystal Structure of Salmonella FlgA in closed form · an experimental structure of the same protein · chain A against B, TM-score 0.87
- 3VJP · Orthorhombic crystal structure of salmonella flga in closed form · an experimental structure of the same protein · chain A against B, TM-score 0.87
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 P40131
- Elsewhere: UniProt P40131 · AlphaFold DB P40131
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