1cqy

X-ray diffraction
1.95Å resolution

STARCH BINDING DOMAIN OF BACILLUS CEREUS BETA-AMYLASE

Released:
Source organism: Bacillus cereus
Entry authors: Yoon HJ, Hirata A, Adachi M, Sekine A, Utsumi S, Mikami B

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-amylase Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.31 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Z4N9 (Residues: 448-546; Coverage: 19%)
Sequence domains: Starch binding domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P3221
Unit cell:
a: 60.195Å b: 60.195Å c: 64.922Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.181 0.225
Expression system: Escherichia coli