3a4a

X-ray diffraction
1.6Å resolution

Crystal structure of isomaltase from Saccharomyces cerevisiae

Released:

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 95.428Å b: 115.404Å c: 61.606Å
α: 90° β: 91.19° γ: 90°
R-values:
R R work R free
0.16 0.159 0.174
Expression system: Escherichia coli