› 4xb3

X-ray diffraction
2.09Å resolution

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: 536 amino acids
Theoretical weight: 62.06 KDa
Source organism: Streptococcus mutans UA159
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99040 (Residues: 1-536; Coverage: 100%)
Gene names: SMU_883, dexB
Sequence domains: Alpha amylase, catalytic domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 4 x CA
Ligand P6G 1 x P6G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 72.151Å b: 82.55Å c: 103.559Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.219
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.
Janeček et al. (2016)
1 more