› 5e9a

X-ray diffraction
2.56Å resolution

Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3

Released:
DOI: 10.2210/pdb5e9a/pdb
PDB entry 5e9a coloured by chain, front view.
PDB entry 5e9a coloured by chain, side view.
PDB entry 5e9a coloured by chain, top view.
Source organism: Rahnella sp. R3
Primary publication:
Cloning, expression and structural stability of a cold-adapted β-galactosidase from Rahnella sp. R3.
Fan Y, Hua X, Zhang Y, Feng Y, Shen Q, Dong J, Zhao W, Zhang W, Jin Z, Yang R
Protein Expr Purif 115 158-64 (2015)
PMID: 26145832

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100989 (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: 712 amino acids
Theoretical weight: 80.28 KDa
Source organism: Rahnella sp. R3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0B4U8I5 (Residues: 1-687; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21
Unit cell:
a: 146.426Å b: 106.831Å c: 164.244Å
α: 90° β: 109° γ: 90°
R-values:
R R work R free
0.2 0.199 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
1 more

6 mentions without citation

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