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AlphaFold monomer V2.0 prediction for beta-XYLOSIDASE/ALPHA-L- arabinofuranosidase 2 (A5JTQ3)

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
A5JTQ3
Type
protein
Length
774 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
Molecule
Beta-XYLOSIDASE/ALPHA-L-arabinofuranosidase 2
UniProt
A5JTQ3
Pockets
5 · best druggability 0.66

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-XYLOSIDASE/ALPHA-L-arabinofuranosidase 2protein77431% helix, 20% strandA5JTQ3

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12670.660.8332empty
22480.570.7842empty
32090.480.7532empty
4660.340.7618empty
5610.310.7614empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

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