› 1j18

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb1j18/pdb
PDB entry 1j18 coloured by chain, front view.
PDB entry 1j18 coloured by chain, side view.
PDB entry 1j18 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Crystal structure of a catalytic site mutant of beta-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose.
Miyake H, Kurisu G, Kusunoki M, Nishimura S, Kitamura S, Nitta Y
Biochemistry 42 5574-81 (2003)
PMID: 12741813

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
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

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, BGC
Carbohydrate polymer
3 bound ligands:
Ligand CA 1 x CA
Ligand SO4 1 x SO4
Ligand ACY 1 x ACY
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)

Quick links

Citations

1 review citation

Clinical applications of amylase: Novel perspectives.
Azzopardi et al. (2016)
7 other articles

1 mention without citation

SN-38-cyclodextrin complexation and its influence on the solubility, stability, and in vitro anticancer activity against ovarian cancer.
Vangara et al. (2014)