Structure of PDB 8ete Chain B

Receptor sequence
>8eteB (length=315) Species: 216816 (Bifidobacterium longum) [Search protein sequence]
CTGVRFSDDEGNTYFGRNLDWSFSYGETILVTPRGYHYDTVFGAGGKAKP
NAVIGVGVVMADRPMYFDCANEHGLAIAGLNFPGYASFVHEPVEGTENVA
TFEFPLWVARNFDSVDEVEETLRNVTLVSQIVPGQQESLLHWFIGDGKRS
IVVEQMADGMHVHHDDVDVLTNQPTFDFHMENLRNYMCVSNEMAEPTSWG
KASLTAWGAGVGMHGIPGDVSSPSRFVRVAYTNAHYPQQNDEAANVSRLF
HTLGSVQMVDGMAKMGDGQFERTLFTSGYSSKTNTYYMNTYDDPAIRSYA
MADYDMDSSELISVA
3D structure
PDB8ete Structural diversity of bile salt hydrolases reveals rationale for substrate selectivity
ChainB
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.-
3.5.1.-
3.5.1.24: choloylglycine hydrolase.
3.5.1.74: chenodeoxycholoyltaurine hydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 WU5 B C2 W22 F68 N82 C1 W21 F67 N81
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016787 hydrolase activity
GO:0045302 choloylglycine hydrolase activity
GO:0047742 chenodeoxycholoyltaurine hydrolase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0006699 bile acid biosynthetic process
Cellular Component
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8ete, PDBe:8ete, PDBj:8ete
PDBsum8ete
PubMed
UniProtQ9KK62|CBH_BIFLN Bile salt hydrolase/transferase (Gene Name=bsh)

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