› 5bn7

X-ray diffraction
3.7Å resolution

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

Released:
DOI: 10.2210/pdb5bn7/pdb
PDB entry 5bn7 coloured by chain, front view.
PDB entry 5bn7 coloured by chain, side view.
PDB entry 5bn7 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein.
Pastor A, Singh AK, Shukla PK, Equbal MJ, Malik ST, Singh TP, Chaudhuri TK
Biochim Biophys Acta 1864 1138-1151 (2016)
PMID: 27317979

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149280 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.33 0.33 0.344
Expression system: Escherichia coli BL21

Quick links

Citations

3 citation in other articles

Preprotein Conformational Dynamics Drive Bivalent Translocase Docking and Secretion.
Sardis et al. (2017)
2 more