PDBe 1bya

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS

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: 495 amino acids
Theoretical weight: 56.07 KDa
Source organism: Glycine max
Expression system: Not provided
UniProt:
  • Canonical: P10538 (Residues: 2-496; Coverage: 100%)
Gene name: BMY1
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 86.2Å b: 86.2Å c: 144.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Not provided