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AlphaFold monomer V2.0 prediction for beta-hexosaminidase (B5RB93)

Analyse AlphaFold monomer V2.0 prediction for beta-hexosaminidase (B5RB93) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B5RB93
Type
protein
Length
341 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x623e0AA2287938657C964a77A11F8Ac724f49e95
Molecule
Beta-hexosaminidase
UniProt
B5RB93
Pockets
1 · best druggability 0.56

Structure

1 distinct chain · 49% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-hexosaminidaseprotein34149% helix, 13% strandB5RB93

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11620.560.8126empty

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