Research workbench
AlphaFold monomer V2.0 prediction for beta-toxin CSE3 (Q95WD2)
Analyse AlphaFold monomer V2.0 prediction for beta-toxin CSE3 (Q95WD2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q95WD2
- Type
- protein
- Length
- 87 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8719F119347D3c1a2ffc2ea3A2408f52f4c89F2A
- Molecule
- Beta-toxin CSE3
- UniProt
- Q95WD2
Structure
1 distinct chain · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-toxin CSE3 | protein | 87 | 26% helix, 24% strand | Q95WD2 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q95WD2
- Elsewhere: UniProt Q95WD2 · AlphaFold DB Q95WD2
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