Function and Biology Details
Reaction catalysed:
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Maltogenic alpha-amylase (preferred)
PDBe Complex ID:
PDB-CPX-148635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Maltogenic alpha-amylase
Molecule details ›
Chain: A
Length: 686 amino acids
Theoretical weight: 75.21 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Bacillus subtilis
UniProt:
Sequence domains:
Length: 686 amino acids
Theoretical weight: 75.21 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Bacillus subtilis
UniProt:
- Canonical:
P19531 (Residues: 34-253, 257-384, 387-719; Coverage: 99%)
Sequence domains:
- Alpha amylase, catalytic domain
- Alpha amylase, C-terminal all-beta domain
- IPT/TIG domain
- Starch binding domain
Ligands and Environments
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU200
Spacegroup:
P3121
Expression system: Bacillus subtilis
