› 1j11

X-ray diffraction
2Å resolution

beta-amylase from Bacillus cereus var. mycoides in complex with alpha-EPG

Released:
DOI: 10.2210/pdb1j11/pdb
PDB entry 1j11 coloured by chain, front view.
PDB entry 1j11 coloured by chain, side view.
PDB entry 1j11 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents.
Oyama T, Miyake H, Kusunoki M, Nitta Y
J Biochem 133 467-74 (2003)
PMID: 12761294

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
Macromolecule:
Beta-amylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 516 amino acids
Theoretical weight: 58.36 KDa
Source organism: Bacillus cereus
UniProt:
  • Canonical: P36924 (Residues: 31-546; Coverage: 100%)
Gene name: spoII
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EPG 4 x EPG
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: C2
Unit cell:
a: 177.9Å b: 112.9Å c: 146.2Å
α: 90° β: 105.8° γ: 90°
R-values:
R R work R free
0.2 0.2 0.246

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Citations

2 review citations

The carbohydrate-binding module family 20--diversity, structure, and function.
Christiansen et al. (2009)
1 more