3mi6

X-ray diffraction
2.7Å resolution

Crystal structure of the alpha-galactosidase from Lactobacillus brevis, Northeast Structural Genomics Consortium Target LbR11.

Released:
Entry authors: Vorobiev S, Chen Y, Seetharaman J, Belote R, Sahdev S, Xiao R, Acton TB, Everett JK, Montelione GT, Hunt JF, Tong L, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169970 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-galactosidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 745 amino acids
Theoretical weight: 86.76 KDa
Source organism: Levilactobacillus brevis ATCC 367
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03PP7 (Residues: 1-737; Coverage: 100%)
Gene name: LVIS_1758
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 115.938Å b: 158.818Å c: 166.017Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.173 0.241
Expression system: Escherichia coli BL21(DE3)