PDBe 3lpo

X-ray diffraction
3.2Å resolution

Crystal structure of the N-terminal domain of sucrase-isomaltase

Released:

Function and Biology Details

Reactions catalysed:
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isomaltase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 898 amino acids
Theoretical weight: 102.87 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P14410 (Residues: 62-931; Coverage: 48%)
Gene name: SI
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 76.344Å b: 172.586Å c: 343.874Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.225 0.251
Expression system: Drosophila melanogaster