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
Sequence domains:
- Alpha amylase
- Legume lectin domain
- Glycosyl hydrolase, family 13, catalytic domain
- Legume lectin, alpha chain, conserved site
- Legume lectin, beta chain, Mn/Ca-binding site
- Concanavalin A-like lectin/glucanase domain superfamily
- Alpha-amylase/branching enzyme, C-terminal all beta
- Alpha-amylase, C-terminal domain
2 more domains
Structure domains:
Structure analysis Details
Assemblies composition:
Assembly name:
Alpha-amylase inhibitor 1 and Alpha-amylase (preferred)
PDBe Complex ID:
PDB-CPX-136282 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Alpha-amylase
Molecule details ›
Chain: A
Length: 471 amino acids
Theoretical weight: 51.23 KDa
Source organism: Tenebrio molitor
UniProt:
Structure domains:
Length: 471 amino acids
Theoretical weight: 51.23 KDa
Source organism: Tenebrio molitor
UniProt:
- Canonical:
P56634 (Residues: 1-471; Coverage: 100%)
Structure domains:
Alpha-amylase inhibitor 1
Molecule details ›
Chain: B
Length: 205 amino acids
Theoretical weight: 22.71 KDa
Source organism: Phaseolus vulgaris
UniProt:
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls
Length: 205 amino acids
Theoretical weight: 22.71 KDa
Source organism: Phaseolus vulgaris
UniProt:
- Canonical: P02873 (Residues: 24-228; Coverage: 92%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls
