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2BJG

Crystal Structure of Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Taurine and Deoxycholate

Functional Information from GO Data
ChainGOidnamespacecontents
A0006629biological_processlipid metabolic process
A0006699biological_processbile acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0045302molecular_functioncholoylglycine hydrolase activity
A0047742molecular_functionchenodeoxycholoyltaurine hydrolase activity
B0006629biological_processlipid metabolic process
B0006699biological_processbile acid biosynthetic process
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
B0045302molecular_functioncholoylglycine hydrolase activity
B0047742molecular_functionchenodeoxycholoyltaurine hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 330
ChainResidue
AASN82
AASN175
BGLY211
BGLN212
BHOH2112

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 331
ChainResidue
BPRO84
AGLY211
AGLN212
AHOH2206
BASN82

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLnFPV
ChainResidueDetails
AALA79-VAL85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:15823032
ChainResidueDetails
ACYS2
BCYS2

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15823032, ECO:0007744|PDB:2BJF
ChainResidueDetails
ACYS2
AARG18
AASN82
BCYS2
BARG18
BASN82

220113

PDB entries from 2024-05-22

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