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AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 3 (G0RA32)

Analyse AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 3 (G0RA32) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
G0RA32
Type
protein
Length
347 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xA528629DC5BcCeBDa9059C9f45aab2F210565E6f
Molecule
Endo-1,4-beta-xylanase 3
UniProt
G0RA32
Pockets
1 · best druggability 0.29

Structure

1 distinct chain · 42% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndo-1,4-beta-xylanase 3protein34742% helix, 16% strandG0RA32

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.290.7514empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4XV0 · Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10)… · an experimental structure of the same protein · chain A against A, TM-score 0.87
  • 4XV0 · Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10)… · an experimental structure of the same protein · chain A against A, TM-score 0.87

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