PDBe 1b1y

X-ray diffraction
2.5Å resolution

SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE

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: 500 amino acids
Theoretical weight: 56.32 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli
UniProt:
  • Canonical: P16098 (Residues: 5-504; Coverage: 94%)
Gene names: AMYB, BMY1
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 72.11Å b: 72.11Å c: 250.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.256
Expression system: Escherichia coli