› 2zic

X-ray diffraction
2.2Å resolution

Crystal structure of Streptococcus mutans dextran glucosidase

Released:
DOI: 10.2210/pdb2zic/pdb
PDB entry 2zic coloured by chain, front view.
PDB entry 2zic coloured by chain, side view.
PDB entry 2zic coloured by chain, top view.
Source organism: Streptococcus mutans
Primary publication:
Substrate recognition mechanism of alpha-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans.
Hondoh H, Saburi W, Mori H, Okuyama M, Nakada T, Matsuura Y, Kimura A
J Mol Biol 378 913-22 (2008)
PMID: 18395742

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha-D-glucans and derived oligosaccharides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189173 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucan 1,6-alpha-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 543 amino acids
Theoretical weight: 63.02 KDa
Source organism: Streptococcus mutans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99040 (Residues: 1-536; Coverage: 100%)
Gene names: SMU_883, dexB
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 3 x CA
Ligand TRS 1 x TRS
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P212121
Unit cell:
a: 72.72Å b: 86.47Å c: 104.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.222
Expression system: Escherichia coli

Quick links

Citations

5 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
4 more

3 mentions without citation

Enzymology and structure of the GH13_31 glucan 1,6-α-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM.
Møller et al. (2012)
2 more