Research workbench
AlphaFold monomer V2.0 prediction for protein sini (P23308)
Analyse AlphaFold monomer V2.0 prediction for protein sini (P23308) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23308
- Type
- protein
- Length
- 57 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Protein sini
- UniProt
- P23308
Structure
1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein sini | protein | 57 | 56% helix, 0% strand | P23308 |
Compared structures
- 1B0N · Sinr PROTEIN/SINI protein complex · an experimental structure of the same protein · chain A against B, TM-score 0.48
- 1B0N · Sinr PROTEIN/SINI protein complex · an experimental structure of the same protein · chain A against B, TM-score 0.48
- 5TMX · Solution structure of sini, antagonist to the master biofilm-regulator sinr in bacillus… · an experimental structure of the same protein · chain A against A, TM-score 0.39
- 5TMX · Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in Bacillus… · an experimental structure of the same protein · chain A against A, TM-score 0.39
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 P23308
- Elsewhere: UniProt P23308 · AlphaFold DB P23308
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