3wau

X-ray diffraction
1.7Å resolution

Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
4-O-beta-D-mannopyranosyl-D-glucopyranose + phosphate = D-glucose + alpha-D-mannose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-177502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-O-beta-D-mannosyl-D-glucose phosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 43.94 KDa
Source organism: Bacteroides fragilis NCTC 9343
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5LH68 (Residues: 1-390; Coverage: 100%)
Gene names: BF0772, BF9343_0737
Sequence domains: beta-1,4-mannooligosaccharide phosphorylase
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: R3
Unit cell:
a: 82.716Å b: 82.716Å c: 308.291Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.234
Expression system: Escherichia coli