7vi7

X-ray diffraction
2Å resolution

Crystal structure of GH3 beta-N-acetylhexosaminidase Amuc_2109 from Akkermansia muciniphila in complex with GlcNAc

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyco_hydro_3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 361 amino acids
Theoretical weight: 39.48 KDa
Source organism: Akkermansia muciniphila ATCC BAA-835
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: B2UPP0 (Residues: 1-353; Coverage: 100%)
Gene name: Amuc_2109
Sequence domains: Glycosyl hydrolase family 3 N terminal domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NFPSS BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 79.243Å b: 81.407Å c: 125.836Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.216
Expression system: Escherichia coli BL21