› 5h3z

X-ray diffraction
2Å resolution

Crystal Structure of 1,2-beta-oligoglucan phosphorylase from Lachnoclostridium phytofermentans

Released:
DOI: 10.2210/pdb5h3z/pdb
PDB entry 5h3z coloured by chain, front view.
PDB entry 5h3z coloured by chain, side view.
PDB entry 5h3z coloured by chain, top view.
Source organism: Lachnoclostridium phytofermentans ISDg
Primary publication:
Mechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentans.
Nakajima M, Tanaka N, Furukawa N, Nihira T, Kodutsumi Y, Takahashi Y, Sugimoto N, Miyanaga A, Fushinobu S, Taguchi H, Nakai H
Sci Rep 7 42671 (2017)
PMID: 28198470

Function and Biology Details

Reaction catalysed: 
((1->2)-beta-D-glucosyl)(n) + phosphate = ((1->2)-beta-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate
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-109003 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 1122 amino acids
Theoretical weight: 128.48 KDa
Source organism: Lachnoclostridium phytofermentans ISDg
Expression system: Escherichia coli
UniProt:
  • Canonical: A9KJS6 (Residues: 2-1113; Coverage: 100%)
Gene name: Cphy_0694
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 10 x GOL
Ligand CA 3 x CA
Ligand PEG 3 x PEG
1 modified residue:
Ligand MSE 38 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 87.761Å b: 94.784Å c: 157.943Å
α: 90° β: 98.41° γ: 90°
R-values:
R R work R free
0.17 0.168 0.204
Expression system: Escherichia coli

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Citations

1 review citation

β-Glucan phosphorylases in carbohydrate synthesis.
Ubiparip et al. (2021)
9 other articles

3 mentions without citation

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