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Crystal structure of GH127 beta-L-arabinofuranosidase HYPBA1 from bifidobacterium longum arabinose complex form

Analyse Crystal structure of GH127 beta-L-arabinofuranosidase HYPBA1 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WKX
Type
protein
Length
657 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Non-reducing end beta-L-arabinofuranosidase
EC
3.2.1.185
UniProt
E8MGH8
Ligands
FUB, ZN
Pockets
4 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANon-reducing end beta-L-arabinofuranosidase (EC 3.2.1.185)protein65740% helix, 18% strandE8MGH8

Ligands and binding sites

  • FUB · beta-L-arabinofuranose · ligand · chains A
  • ZN · Zinc ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14190.700.8268FUB
23840.670.8036empty
32950.580.7733empty
4540.350.7821empty

Compared structures

  • 3WKX · Crystal structure of GH127 beta-L-arabinofuranosidase HypBA1 from Bifidobacterium longum… · the same entry in another collection · chain A against A, TM-score 1.00
  • E8MGH8 · AlphaFold monomer V2.0 prediction for non-reducing end beta-L- arabinofuranosidase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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