Function and Biology Details
Reaction catalysed:
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose
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:
Maltase-glucoamylase (preferred)
PDBe Complex ID:
PDB-CPX-128929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Maltase-glucoamylase
Molecule details ›
Chain: A
Length: 870 amino acids
Theoretical weight: 98.59 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
Sequence domains:
Length: 870 amino acids
Theoretical weight: 98.59 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
- Canonical:
O43451 (Residues: 87-954; Coverage: 32%)
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
Experiments and Validation Details
X-ray source:
CHESS BEAMLINE F1
Spacegroup:
P212121
Expression system: Drosophila melanogaster
