› 1gow

X-ray diffraction
2.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149650 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 489 amino acids
Theoretical weight: 56.77 KDa
Source organism: Saccharolobus solfataricus
UniProt:
  • Canonical: P22498 (Residues: 1-489; Coverage: 100%)
Gene names: SSO3019, lacS
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P3121
Unit cell:
a: 169.4Å b: 169.4Å c: 98.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.219 0.259

Quick links

Citations

17 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
16 more

8 mentions without citation

Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution.
Omelchenko et al. (2010)
7 more