PDBe 2qmj

X-ray diffraction
1.9Å resolution

Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose


Function and Biology Details

Reactions catalysed:
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Maltase-glucoamylase, intestinal Chain: A
Molecule details ›
Chain: A
Length: 870 amino acids
Theoretical weight: 98.59 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
  • Canonical: O43451 (Residues: 87-954; Coverage: 47%)
Gene names: MGA, MGAM, MGAML
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 86.97Å b: 109.367Å c: 109.271Å
α: 90° β: 90° γ: 90°
R R work R free
0.179 0.177 0.215
Expression system: Drosophila melanogaster