PDBe 1j18

X-ray diffraction
2Å resolution

Crystal Structure of a Beta-Amylase from Bacillus cereus var. mycoides Cocrystallized with Maltose

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 516 amino acids
Theoretical weight: 58.36 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36924 (Residues: 31-546; Coverage: 100%)
Gene name: spoII
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P21
Unit cell:
a: 56.808Å b: 89.331Å c: 65.394Å
α: 90° β: 102.32° γ: 90°
R-values:
R R work R free
0.181 0.181 0.221
Expression system: Escherichia coli BL21(DE3)