5hke

X-ray diffraction
1.9Å resolution

bile salt hydrolase from Lactobacillus salivarius

Released:
Source organism: Lactobacillus salivarius
Primary publication:
Crystal structure of bile salt hydrolase from Lactobacillus salivarius.
Acta Crystallogr F Struct Biol Commun 72 376-81 (2016)
PMID: 27139829

Function and Biology Details

Reaction catalysed:
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholan-24-oylglycine + H(2)O = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + glycine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CBAH domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 37.93 KDa
Source organism: Lactobacillus salivarius
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: J7H3P9 (Residues: 1-324; Coverage: 100%)
Sequence domains: Linear amide C-N hydrolases, choloylglycine hydrolase family
Structure domains: Penicillin V Acylase; Chain A

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21212
Unit cell:
a: 90.79Å b: 87.356Å c: 86.766Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.152 0.185
Expression system: Escherichia coli BL21(DE3)