Research workbench
AlphaFold monomer V2.0 prediction for delta-hemolysin (P0C1V1)
Analyse AlphaFold monomer V2.0 prediction for delta-hemolysin (P0C1V1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0C1V1
- Type
- protein
- Length
- 26 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- UniProt
- P0C1V1
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 26 | — | P0C1V1 |
Compared structures
- 2KAM · NMR structure of delta-toxin from Staphylococcus aureus in CD3OH · an experimental structure of the same protein · chain A against A, TM-score 0.66
- 2KAM · NMR structure of delta-toxin from staphylococcus aureus in CD3OH · an experimental structure of the same protein · chain A against A, TM-score 0.66
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 P0C1V1
- Elsewhere: UniProt P0C1V1 · AlphaFold DB P0C1V1
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