Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1G24

THE CRYSTAL STRUCTURE OF EXOENZYME C3 FROM CLOSTRIDIUM BOTULINUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
B0005576cellular_componentextracellular region
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
C0005576cellular_componentextracellular region
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
D0005576cellular_componentextracellular region
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues796
DetailsDomain: {"description":"TR mART core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues52
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12029083","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16177825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11114250
ChainResidueDetails
AGLU214

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11114250
ChainResidueDetails
BGLU1214

site_idCSA3
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11114250
ChainResidueDetails
CGLU2214

site_idCSA4
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11114250
ChainResidueDetails
DGLU3214

site_idMCSA1
Number of Residues2
DetailsM-CSA 824
ChainResidueDetails
ASER174electrostatic stabiliser, polar interaction
AGLU214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 824
ChainResidueDetails
BSER1174electrostatic stabiliser, polar interaction
BGLU1214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 824
ChainResidueDetails
CSER2174electrostatic stabiliser, polar interaction
CGLU2214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

site_idMCSA4
Number of Residues2
DetailsM-CSA 824
ChainResidueDetails
DSER3174electrostatic stabiliser, polar interaction
DGLU3214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon