Function and Biology Details
Reactions 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
Chenodeoxycholoyltaurine + H(2)O = chenodeoxycholate + taurine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
homo tetramer (preferred)
Assembly name:
Bile salt hydrolase/transferase (preferred)
PDBe Complex ID:
PDB-CPX-191912 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bile salt hydrolase/transferase
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.05 KDa
Source organism: Bifidobacterium longum
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Linear amide C-N hydrolases, choloylglycine hydrolase family
Structure domains: Penicillin V Acylase; Chain A
Length: 316 amino acids
Theoretical weight: 35.05 KDa
Source organism: Bifidobacterium longum
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9KK62 (Residues: 2-317; Coverage: 100%)
Sequence domains: Linear amide C-N hydrolases, choloylglycine hydrolase family
Structure domains: Penicillin V Acylase; Chain A
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
ESRF BEAMLINE BM14
Spacegroup:
P6122
Expression system: Escherichia coli BL21(DE3)
