Research workbench
AlphaFold monomer V2.0 prediction for flagellar assembly factor fliw (A4ISV0)
Analyse AlphaFold monomer V2.0 prediction for flagellar assembly factor fliw (A4ISV0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4ISV0
- Type
- protein
- Length
- 144 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- UniProt
- A4ISV0
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 144 | — | A4ISV0 |
Compared structures
- 5DMD · Crystal structure of the flagellar assembly factor FliW · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 5DMD · Crystal structure of the flagellar assembly factor fliw · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 5DMB · Crystal structure of a translational regulator bound to a flagellar assembly factor · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 5DMB · Crystal structure of a translational regulator bound to a flagellar assembly factor · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 5JAK · Crystal structure of the flagellar assembly factor fliw · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 5JAK · Crystal structure of the flagellar assembly factor FliW · an experimental structure of the same protein · chain A against A, TM-score 0.92
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 A4ISV0
- Elsewhere: UniProt A4ISV0 · AlphaFold DB A4ISV0
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