› 6zjt

X-ray diffraction
1.97Å resolution

Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB mutant E441Q in complex with lactulose

Released:
DOI: 10.2210/pdb6zjt/pdb
PDB entry 6zjt coloured by chain, front view.
PDB entry 6zjt coloured by chain, side view.
PDB entry 6zjt coloured by chain, top view.
Source organism: Arthrobacter sp. 32cB
Primary publication:
Mapping the Transglycosylation Relevant Sites of Cold-Adapted β-d-Galactosidase from Arthrobacter sp. 32cB.
Rutkiewicz M, Wanarska M, Bujacz A
OpenAccess logo Int J Mol Sci 21 (2020)
PMID: 32731412

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100055 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
beta-galactosidase Chain: A
Molecule details ›
Chain: A
Length: 1010 amino acids
Theoretical weight: 109.76 KDa
Source organism: Arthrobacter sp. 32cB
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A023UGN9 (Residues: 1-1010; Coverage: 100%)
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GAL, FRU
Carbohydrate polymer
3 bound ligands:
Ligand GAL 2 x GAL
Ligand ACT 2 x ACT
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P3121
Unit cell:
a: 138.974Å b: 138.974Å c: 127.699Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.226
Expression system: Escherichia coli

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Citations

3 review citations

Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast, Glaciozyma antarctica PI12.
Yusof et al. (2021)
2 more

1 mention without citation

Mapping the Transglycosylation Relevant Sites of Cold-Adapted β-d-Galactosidase from Arthrobacter sp. 32cB.
Rutkiewicz et al. (2020)