› 1b90

X-ray diffraction
2.5Å resolution

BACILLUS CEREUS BETA-AMYLASE APO FORM

Released:
DOI: 10.2210/pdb1b90/pdb
PDB entry 1b90 coloured by chain, front view.
PDB entry 1b90 coloured by chain, side view.
PDB entry 1b90 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose.
Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S
Biochemistry 38 7050-61 (1999)
PMID: 10353816

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 Chain: A
Molecule details ›
Chain: A
Length: 516 amino acids
Theoretical weight: 58.36 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:
Ligand ACT 1 x ACT
Ligand SO4 1 x SO4
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 57.075Å b: 92.103Å c: 65.671Å
α: 90° β: 101.81° γ: 90°
R-values:
R R work R free
0.164 0.164 0.247
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
5 more

5 mentions without citation

Selective prediction of interaction sites in protein structures with THEMATICS.
Wei et al. (2007)
4 more