Structure analysis

Bifidobacterium longum bile salt hydrolase

X-ray diffraction
2.5Å resolution
Source organism: Bifidobacterium longum
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 44568.31 Å2
Buried surface area: 15771.82 Å2
Dissociation area: 3,786.7 Å2
Dissociation energy (ΔGdiss): 71.09 kcal/mol
Dissociation entropy (TΔSdiss): 15.45 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-191912
    Assembly 1
Confidence : 98%
No. subunits : 4
Symmetry : D2
3DComplex & QSbio predictionx
No. subunits : 4
Symmetry : D2

Macromolecules

Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.1 KDa
Source organism: Bifidobacterium longum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KK62 (Residues: 2-317; Coverage: 100%)
Gene name: bsh
Pfam: Linear amide C-N hydrolases, choloylglycine hydrolase family
InterPro:
CATH: Penicillin V Acylase; Chain A
PDBe-KB: UniProt Coverage View: Q9KK62  
131620406080100120140160180200220240260280300
 
100200300
UniProt
Q9KK62
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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