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AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 2 (Q9HGE1)

Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 2 (Q9HGE1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q9HGE1
Type
protein
Length
227 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xf82721010A87D54712b6c5deC75cb63B8BF88c23
Molecule
Endo-1,4-beta-xylanase 2
UniProt
Q9HGE1
Pockets
1 · best druggability 0.57

Structure

1 distinct chain · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndo-1,4-beta-xylanase 2protein2276% helix, 52% strandQ9HGE1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12120.570.8031empty

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