Structure of PDB 8ete Chain A

Receptor sequence
>8eteA (length=310) Species: 216816 (Bifidobacterium longum) [Search protein sequence]
CTGVRFSDDEGNTYFGRNLDWSFSYGETILVTPRGYHYDTVFGAGGKAKP
NAVIGVGVVMADRPMYFDCANEHGLAIAGLNFPGYASFVHEPVEGTENVA
TFEFPLWVARNFDSVDEVEETLRNVTLVSQQESLLHWFIGDGKRSIVVEQ
MADGMHVHHDDVDVLTNQPTFDFHMENLRNYMCVSNEMAEPTSWGKASLT
AWGAGVGMHGIPGDVSSPSRFVRVAYTNAHYPQQNDEAANVSRLFHTLGS
VQMVDGMAKMGDGQFERTLFTSGYSSKTNTYYMNTYDDPAIRSYAMADYD
MDSSELISVA
3D structure
PDB8ete Structural diversity of bile salt hydrolases reveals rationale for substrate selectivity
ChainA
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A C2 Y26 F68 N82 F103 S139 C1 Y25 F67 N81 F102 S133
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

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

[Back to BioLiP]