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2BJF

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE DXC A 330
ChainResidue
ACYS2
AGLU135
AILE137
APRO138
ATHR140
ALEU142
AHOH2017
AARG18
AMET20
ATYR24
APHE26
APHE61
AGLY80
AASN82
AILE133

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TAU A 331
ChainResidue
AASN82
APRO84
AGLY211
AGLN212
AHOH2188
AHOH2241
AHOH2309
AHOH2310

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 332
ChainResidue
ATYR86
APRO177
ATHR178
AASP180
ATRP181
AHOH2155

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 333
ChainResidue
AASP248
ALEU249
ALYS286
ATYR290
AHOH2009
AHOH2312

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 Residues1
DetailsACT_SITE: Nucleophile; acyl-thioester intermediate => ECO:0000305|PubMed:15823032, ECO:0000305|PubMed:38326608
ChainResidueDetails
ACYS2

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15823032, ECO:0007744|PDB:2BJF
ChainResidueDetails
ACYS2
AARG18
AASN82

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PDB entries from 2024-11-06

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