PDBe 1uko

X-ray diffraction
2.1Å resolution

Crystal structure of soybean beta-amylase mutant substituted at surface region

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 495 amino acids
Theoretical weight: 56.08 KDa
Source organism: Glycine max
Expression system: Escherichia coli
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
X-ray source: MACSCIENCE
Spacegroup: P1
Unit cell:
a: 75.1Å b: 78.14Å c: 87.944Å
α: 89.93° β: 89.88° γ: 90.08°
R-values:
R R work R free
0.183 0.183 0.241
Expression system: Escherichia coli