4cu9

X-ray diffraction
1.83Å resolution

Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae beta-galactosidase, BgaA

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 20.98 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DQP4 (Residues: 1822-1998; Coverage: 8%)
Gene names: bgaA, spr0565
Sequence domains: Beta-galactosidase-like, Galactose-binding domain
Structure domains: Galactose-binding domain-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P212121
Unit cell:
a: 38.25Å b: 69.28Å c: 121.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.217
Expression system: Escherichia coli