PDBe 1vep

X-ray diffraction
2.06Å resolution

Crystal Structure Analysis of Triple (T47M/Y164E/T328N)/maltose of Bacillus cereus Beta-Amylase at pH 6.5

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: 58.37 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: P36924 (Residues: 31-546; Coverage: 100%)
Gene name: spoII
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P21
Unit cell:
a: 57.45Å b: 92.695Å c: 65.755Å
α: 90° β: 102.37° γ: 90°
R-values:
R R work R free
0.183 0.183 0.226
Expression system: Escherichia coli