› 3axh

X-ray diffraction
1.8Å resolution

Crystal structure of isomaltase in complex with isomaltose

Released:
DOI: 10.2210/pdb3axh/pdb
PDB entry 3axh coloured by chain, front view.
PDB entry 3axh coloured by chain, side view.
PDB entry 3axh coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Steric hindrance by 2 amino acid residues determines the substrate specificity of isomaltase from Saccharomyces cerevisiae.
Yamamoto K, Miyake H, Kusunoki M, Osaki S
J Biosci Bioeng 112 545-50 (2011)
PMID: 21925939

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
Macromolecules (2 distinct):
Oligo-1,6-glucosidase IMA1 Chain: A
Molecule details ›
Chain: A
Length: 589 amino acids
Theoretical weight: 68.62 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

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 94.892Å b: 114.736Å c: 61.496Å
α: 90° β: 90.99° γ: 90°
R-values:
R R work R free
0.169 0.168 0.193
Expression system: Escherichia coli

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Citations

2 review citations

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

22 mentions without citation

Dynamical origins of heat capacity changes in enzyme-catalysed reactions.
van der Kamp et al. (2018)
21 more