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3BSW

PglD-citrate complex, from Campylobacter jejuni NCTC 11168

Functional Information from GO Data
ChainGOidnamespacecontents
A0006486biological_processprotein glycosylation
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0018279biological_processprotein N-linked glycosylation via asparagine
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CIT A 201
ChainResidue
AASN118
AHOH207
AHOH326
AHOH360
AHOH370
AHOH394
AHOH405
AGLU124
AHIS134
ASER136
AALA142
AGLY143
AILE155
APRO161
AHOH203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18667421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18667421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Increases basicity of active site His"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AHIS125

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
APRO161

238895

PDB entries from 2025-07-16

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