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Native structure of the GH93 alpha-L-arabinofuranosidase of fusarium graminearum

Analyse Native structure of the GH93 alpha-L-arabinofuranosidase of fusarium graminearum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W5N
Type
protein
Length
365 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-L-arabinofuranosidase
EC
3.2.1.55
Pockets
3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-L-arabinofuranosidase (EC 3.2.1.55)protein3651% helix, 45% strand—

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · chains A
  • PGE · Triethylene glycol · additive · chains A
  • GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14810.700.8031empty
22260.550.7732GOL
3540.330.7715empty

Compared structures

  • 2W5N · Native structure of the GH93 alpha-L-arabinofuranosidase of Fusarium graminearum · the same entry in another collection · chain A against A, TM-score 1.00

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