› 4wlc

X-ray diffraction
2.4Å 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:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand BGC 1 x BGC
Ligand GOL 2 x GOL
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 72.989Å b: 83.736Å c: 103.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.263
Expression system: Escherichia coli

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Citations

2 review citations

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