› 5zcb

X-ray diffraction
2.5Å resolution

Crystal structure of Alpha-glucosidase

Released:
DOI: 10.2210/pdb5zcb/pdb
PDB entry 5zcb coloured by chain, front view.
PDB entry 5zcb coloured by chain, side view.
PDB entry 5zcb coloured by chain, top view.
Source organism: Bacillus sp. (in: Bacteria)
Primary publication:
Function and structure of GH13_31 α-glucosidase with high α-(1→4)-glucosidic linkage specificity and transglucosylation activity.
Auiewiriyanukul W, Saburi W, Kato K, Yao M, Mori H
FEBS Lett 592 2268-2281 (2018)
PMID: 29870070

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 555 amino acids
Theoretical weight: 64.93 KDa
Source organism: Bacillus sp. (in: Bacteria)
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 54.893Å b: 84.856Å c: 128.429Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.215
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Dietary Polyphenols as Natural Inhibitors of α-Amylase and α-Glucosidase.
Ćorković et al. (2022)
1 more

4 mentions without citation

Phytochemical Profiling, In Vitro Biological Activities, and In-Silico Studies of Ficus vasta Forssk.: An Unexplored Plant.
Aati et al. (2022)
3 more