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:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Beta-amylase Tri a 17 (preferred)
PDBe Complex ID:
PDB-CPX-161085 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-amylase Tri a 17
Molecule details ›
Chain: A
Length: 509 amino acids
Theoretical weight: 57.51 KDa
Source organism: Triticum aestivum
Expression system: Escherichia coli
UniProt:
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases
Length: 509 amino acids
Theoretical weight: 57.51 KDa
Source organism: Triticum aestivum
Expression system: Escherichia coli
UniProt:
- Canonical:
P93594 (Residues: 1-503; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 14
Structure domains: Glycosidases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ELETTRA BEAMLINE 5.2R
Spacegroup:
P43
Expression system: Escherichia coli
