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AlphaFold monomer V2.0 prediction for syndecan-3 (P26261)

Analyse AlphaFold monomer V2.0 prediction for syndecan-3 (P26261) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P26261
Type
protein
Length
405 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
Molecule
Syndecan-3
UniProt
P26261

Structure

1 distinct chain · 13% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASyndecan-3protein40513% helix, 0% strandP26261

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