Research workbench
AlphaFold monomer V2.0 prediction for flagellar P-ring protein (C3MG26)
Analyse AlphaFold monomer V2.0 prediction for flagellar P-ring protein (C3MG26) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3MG26
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2F6bF430f3601bBa63610839f7537AE491c6C9Fe
- UniProt
- C3MG26
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 371 | — | C3MG26 |
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 C3MG26
- Elsewhere: UniProt C3MG26 · AlphaFold DB C3MG26
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