PDBe 2xfr

X-ray diffraction
0.97Å resolution

Crystal structure of barley beta-amylase at atomic resolution

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: 535 amino acids
Theoretical weight: 59.67 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P16098 (Residues: 1-535; Coverage: 100%)
Gene names: AMYB, 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: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 68.83Å b: 71.338Å c: 92.659Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.114 0.113 0.13