› 3ton

X-ray diffraction
2.95Å resolution

Crystral Structure of the C-terminal Subunit of Human Maltase-Glucoamylase

Released:
DOI: 10.2210/pdb3ton/pdb
PDB entry 3ton coloured by chain, front view.
PDB entry 3ton coloured by chain, side view.
PDB entry 3ton 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
Macromolecule:
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43212
Unit cell:
a: 106.232Å b: 106.232Å c: 517.557Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.232 0.288
Expression system: Komagataella pastoris

Quick links

Citations

8 review citations

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

10 mentions without citation

A comprehensive overview of substrate specificity of glycoside hydrolases and transporters in the small intestine : "A gut feeling".
Elferink et al. (2020)
9 more