1e43

X-ray diffraction
1.7Å resolution

Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A

Released:

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 55.04 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus amyloliquefaciens
UniProt:
  • Canonical: P00692 (Residues: 32-514; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 52.2Å b: 76.1Å c: 236.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.133 0.185
Expression system: Bacillus amyloliquefaciens