Function and Biology Details
Reaction catalysed:
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Alpha-amylase (preferred)
PDBe Complex ID:
PDB-CPX-138988 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-amylase
Molecule details ›
Chain: A
Length: 189 amino acids
Theoretical weight: 21.81 KDa
Source organism: Bacillus licheniformis
UniProt:
Sequence domains: Alpha amylase, catalytic domain
Structure domains:
Length: 189 amino acids
Theoretical weight: 21.81 KDa
Source organism: Bacillus licheniformis
UniProt:
- Canonical:
P06278 (Residues: 30-218; Coverage: 39%)
Sequence domains: Alpha amylase, catalytic domain
Structure domains:
Alpha-amylase
Molecule details ›
Chain: B
Length: 294 amino acids
Theoretical weight: 33.51 KDa
Source organism: Bacillus licheniformis
UniProt:
Sequence domains:
Structure domains: Golgi alpha-mannosidase II
Length: 294 amino acids
Theoretical weight: 33.51 KDa
Source organism: Bacillus licheniformis
UniProt:
- Canonical: P06278 (Residues: 219-512; Coverage: 61%)
Sequence domains:
Structure domains: Golgi alpha-mannosidase II
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P43212
