› 3aj7

X-ray diffraction
1.3Å resolution

Crystal Structure of isomaltase from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb3aj7/pdb
PDB entry 3aj7 coloured by chain, front view.
PDB entry 3aj7 coloured by chain, side view.
PDB entry 3aj7 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose.
Yamamoto K, Miyake H, Kusunoki M, Osaki S
FEBS J 277 4205-14 (2010)
PMID: 20812985

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oligo-1,6-glucosidase IMA1 Chain: A
Molecule details ›
Chain: A
Length: 589 amino acids
Theoretical weight: 68.68 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53051 (Residues: 1-589; Coverage: 100%)
Gene names: IMA1, YGR287C
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2
Unit cell:
a: 95.516Å b: 115.538Å c: 61.756Å
α: 90° β: 91.05° γ: 90°
R-values:
R R work R free
0.173 0.172 0.186
Expression system: Escherichia coli

Quick links

Citations

5 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
4 more

34 mentions without citation

An overview on the role of bioactive α-glucosidase inhibitors in ameliorating diabetic complications.
Hossain et al. (2020)
33 more