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2RF8

Crystal Structure of the mutant C2A conjugated bile acid hydrolase from Clostridium perfringens

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 Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 332
ChainResidue
AALA2
AASN82
APRO84
AASN175
AARG228
AMET261
BGLN212

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 333
ChainResidue
BMET1
BASN82
BPRO84
BASN175
BPRO225
BHOH373
BHOH379
ALEU210
AGLY211

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 334
ChainResidue
AASN36
ALYS38
AASN312
AHOH419

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; acyl-thioester intermediate => ECO:0000305|PubMed:15823032, ECO:0000305|PubMed:38326608
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15823032, ECO:0007744|PDB:2BJF
ChainResidueDetails
AALA2
AARG18
AASN82
BALA2
BARG18
BASN82

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PDB entries from 2024-07-17

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