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AlphaFold monomer V2.0 prediction for beta-XYLOSIDASE/ALPHA-L- arabinofuranosidase 1 (A5JTQ2)

Analyse AlphaFold monomer V2.0 prediction for beta-XYLOSIDASE/ALPHA-L… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A5JTQ2
Type
protein
Length
774 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xe43D264c0E4229A2c42bC24F7Fed41a1fCf1938d
Molecule
Beta-XYLOSIDASE/ALPHA-L-arabinofuranosidase 1
UniProt
A5JTQ2
Pockets
4 · best druggability 0.60

Structure

1 distinct chain · 31% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-XYLOSIDASE/ALPHA-L-arabinofuranosidase 1protein77431% helix, 20% strandA5JTQ2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13700.600.7746empty
22360.490.7533empty
3930.420.7817empty
4610.290.7416empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

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