Function and Biology Details
Reactions catalysed:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- P-type trefoil domain
- Glycosyl hydrolase, all-beta
- Glycosyl hydrolases family 31, conserved site
- Glycosyl hydrolases family 31, active site
- Glycoside hydrolase superfamily
- Glycoside hydrolase family 31, TIM barrel domain
- Galactose mutarotase-like domain superfamily
- P-type trefoil, conserved site
1 more domain
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Isomaltase (preferred)
PDBe Complex ID:
PDB-CPX-146939 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Isomaltase
Molecule details ›
Chains: A, B, C, D
Length: 898 amino acids
Theoretical weight: 102.87 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
Sequence domains:
Length: 898 amino acids
Theoretical weight: 102.87 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
- Canonical:
P14410 (Residues: 62-931; Coverage: 48%)
Sequence domains:
- Trefoil (P-type) domain
- Glycosyl hydrolase 31 N-terminal galactose mutarotase-like domain
- Glycosyl hydrolases family 31 TIM-barrel domain
- Glycosyl hydrolase family 31 C-terminal domain
Ligands and Environments
1 bound ligand:
No modified residues
Experiments and Validation Details
X-ray source:
CHESS BEAMLINE F1
Spacegroup:
P212121
Expression system: Drosophila melanogaster
