› 5vqd

X-ray diffraction
2.1Å resolution

Beta-glucoside phosphorylase BglX

Released:
DOI: 10.2210/pdb5vqd/pdb
Model geometry
Fit model/data
PDB entry 5vqd coloured by chain, front view.
PDB entry 5vqd coloured by chain, side view.
PDB entry 5vqd coloured by chain, top view.
Source organism: unidentified
Primary publication:
Structural and mechanistic analysis of a β-glycoside phosphorylase identified by screening a metagenomic library.
Macdonald SS, Patel A, Larmour VLC, Morgan-Lang C, Hallam SJ, Mark BL, Withers SG
J Biol Chem 293 3451-3467 (2018)
PMID: 29317495

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-104420 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-N-acetylhexosaminidase Chain: A
Molecule details ›
Chain: A
Length: 573 amino acids
Theoretical weight: 64.67 KDa
Source organism: unidentified
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2R2JFS5 (Residues: 1-573; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 3 N terminal domain

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 80.52Å b: 84.15Å c: 161.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.204 0.257
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Harnessing glycoenzyme engineering for synthesis of bioactive oligosaccharides.
Benkoulouche et al. (2019)
1 more

3 mentions without citation

Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.
Li et al. (2022)
2 more