› 3top

X-ray diffraction
2.88Å resolution

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

Released:
DOI: 10.2210/pdb3top/pdb
PDB entry 3top coloured by chain, front view.
PDB entry 3top coloured by chain, side view.
PDB entry 3top coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insight into substrate specificity of human intestinal maltase-glucoamylase.
Ren L, Qin X, Cao X, Wang L, Bai F, Bai G, Shen Y
Protein Cell 2 827-36 (2011)
PMID: 22058037

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltase-glucoamylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 908 amino acids
Theoretical weight: 103.73 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: O43451 (Residues: 1856-2749; Coverage: 33%)
Gene names: MGA, MGAM, MGAML
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, AC1
Ligand GLC 4 x GLC
Ligand AC1 2 x AC1
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43212
Unit cell:
a: 105.501Å b: 105.501Å c: 516.561Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.218 0.284
Expression system: Komagataella pastoris

Quick links

Citations

5 review citations

α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.
Okuyama et al. (2016)
4 more

60 mentions without citation

Recent Updates on Phytoconstituent Alpha-Glucosidase Inhibitors: An Approach towards the Treatment of Type Two Diabetes.
Kashtoh et al. (2022)
59 more