X-ray diffraction
2.21Å resolution

Crystal Structure Analysis of Alpha-Amylase from Bacillus Subtilis complexed with Acarbose

Source organism: Bacillus subtilis

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 46.8 KDa
Source organism: Bacillus subtilis
Expression system: Bacillus subtilis
  • Canonical: P00691 (Residues: 45-466; Coverage: 67%)
Gene names: BSU03040, amyA, amyE
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, GLD
Carbohydrate polymer : NEW Components: BGC, G6D
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P212121
Unit cell:
a: 70.32Å b: 74.204Å c: 115.724Å
α: 90° β: 90° γ: 90°
R R work R free
0.208 0.208 0.265
Expression system: Bacillus subtilis