3uet

X-ray diffraction
2.1Å resolution

Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->3)-linkages between alpha-L-fucose and N-acetylglucosamine residues in glycoproteins
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-110471 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
F5/8 type C domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 478 amino acids
Theoretical weight: 52.99 KDa
Source organism: Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088
Expression system: Escherichia coli
UniProt:
  • Canonical: B7GNN8 (Residues: 1-478; Coverage: 100%)
Gene name: Blon_2336
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, GAL, FUC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 82.588Å b: 105.971Å c: 120.715Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.223
Expression system: Escherichia coli