Research workbench
AlphaFold monomer V2.0 prediction for syndecan-1 (P26260)
Analyse AlphaFold monomer V2.0 prediction for syndecan-1 (P26260) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P26260
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3c5FaA97b7dc26B6aC1bAEa31C061F5c41fF8D21
- Molecule
- Syndecan-1
- UniProt
- P26260
Structure
1 distinct chain · 17% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Syndecan-1 | protein | 313 | 17% helix, 0% strand | P26260 |
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 P26260
- Elsewhere: UniProt P26260 · AlphaFold DB P26260
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