X-ray diffraction
3.7Å resolution

Crystal structure of maltodextrin glucosidase from E.coli at 3.7 A resolution


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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Maltodextrin glucosidase Chain: A
Molecule details ›
Chain: A
Length: 616 amino acids
Theoretical weight: 70.53 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
  • Canonical: P21517 (Residues: 1-604; Coverage: 100%)
Gene names: JW0393, b0403, malZ
Sequence domains:
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P4
Unit cell:
a: 110.59Å b: 110.59Å c: 69.54Å
α: 90° β: 90° γ: 90°
R R work R free
0.33 0.33 0.344
Expression system: Escherichia coli BL21