› 6lgg

X-ray diffraction
1.84Å resolution

Bombyx mori GH13 sucrose hydrolase mutant E322Q complexed with sucrose

Released:
DOI: 10.2210/pdb6lgg/pdb
PDB entry 6lgg coloured by chain, front view.
PDB entry 6lgg coloured by chain, side view.
PDB entry 6lgg coloured by chain, top view.
Source organism: Bombyx mori
Primary publication:
Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-α-glucosidases.
Miyazaki T, Park EY
J Biol Chem 295 8784-8797 (2020)
PMID: 32381508

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose
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-492608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
alpha-glucosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 598 amino acids
Theoretical weight: 68.74 KDa
Source organism: Bombyx mori
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A077JI83 (Residues: 30-606; Coverage: 95%)
Gene names: 101745623, BmSuh
Sequence domains: Alpha amylase, catalytic domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
2 bound ligands:
Ligand MG 4 x MG
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 64.7Å b: 127.9Å c: 154.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The chemistry and biology of natural ribomimetics and related compounds.
Tsunoda et al. (2022)
4 other articles

1 mention without citation

Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-α-glucosidases.
Miyazaki et al. (2020)