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2RLC

Crystal Structure of the Conjugated Bile Acid Hydrolase from Clostridium perfringens in Complex with Reaction Products Glycine and Cholate

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 330
ChainResidue
AASP243
AARG263
AARG267
ASER273
AHOH427
AHOH684
AHOH686

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 331
ChainResidue
AHOH540
AHOH689
AHOH692
AASN308
ALYS315

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CHD A 332
ChainResidue
AOCS2
AARG18
AMSE20
APHE26
APHE61
AGLY80
AGLU135
AILE137
ATHR140
ALEU142

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GLY A 333
ChainResidue
AOCS2
AASN82
AASN175
AGLY211
AGLN212
AHOH365
AHOH597

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
AOCS2

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15823032, ECO:0007744|PDB:2BJF
ChainResidueDetails
AOCS2
AARG18
AASN82

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PDB entries from 2024-07-24

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