› 3tty

X-ray diffraction
2.25Å resolution

Crystal structure of beta-galactosidase from Bacillus circulans sp. alkalophilus in complex with galactose

Released:
DOI: 10.2210/pdb3tty/pdb
PDB entry 3tty coloured by chain, front view.
PDB entry 3tty coloured by chain, side view.
PDB entry 3tty coloured by chain, top view.
Source organism: Niallia circulans subsp. alkalophilus
Primary publication:
Structural analysis, enzymatic characterization, and catalytic mechanisms of β-galactosidase from Bacillus circulans sp. alkalophilus.
Maksimainen M, Paavilainen S, Hakulinen N, Rouvinen J
FEBS J 279 1788-98 (2012)
PMID: 22385475

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-164089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-galactosidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 675 amino acids
Theoretical weight: 77.41 KDa
Source organism: Niallia circulans subsp. alkalophilus
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 6 x ZN
Ligand GLA 6 x GLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: R3
Unit cell:
a: 228.2Å b: 228.2Å c: 246.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.16 0.21

Quick links

Citations

3 review citations

Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.
Mangiagalli et al. (2021)
2 more

5 mentions without citation

Structural Insights into the Molecular Evolution of the Archaeal Exo-β-d-Glucosaminidase.
Mine et al. (2019)
4 more