› 6ggy

X-ray diffraction
1.95Å resolution

Function and Biology Details

Reaction catalysed: 
3-beta-D-glucosyl-D-glucose + phosphate = D-glucose + alpha-D-glucose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laminaribiose phosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 913 amino acids
Theoretical weight: 101.87 KDa
Source organism: Paenibacillus sp. YM1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D7UT17 (Residues: 1-911; Coverage: 100%)
Gene name: lbpA
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 4 x SO4
Ligand EDO 10 x EDO
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41212
Unit cell:
a: 146.704Å b: 146.704Å c: 222.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.223
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Recent advances in enzymatic synthesis of β-glucan and cellulose.
Bulmer et al. (2021)
2 more

2 mentions without citation

Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution.
Sun et al. (2021)
1 more