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1UZI

C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE VO4 A1002
ChainResidue
ALYS81
APRO101
ASER102
AHOH2153
AHOH2154
AHOH2155

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE VO4 A1003
ChainResidue
AGOL1004
AGOL1005
BSER69
BLYS70
BSER71
ASER69
ALYS70
ASER71

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE VO4 B1002
ChainResidue
BLYS81
BPRO101
BSER102
BHOH2150
BHOH2151
BHOH2152

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE V4O A1001
ChainResidue
AASN145
AILE150
AASN151
ALYS152
ATHR153
BASN145
BILE150
BASN151
BLYS152

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1004
ChainResidue
ASER69
ASER71
AVO41003
BLYS70

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1005
ChainResidue
ALYS70
AVO41003
BSER69
BSER71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues398
DetailsDomain: {"description":"TR mART core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12029083","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16177825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g24
ChainResidueDetails
AGLU214

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g24
ChainResidueDetails
BGLU214

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
BSER174electrostatic stabiliser, polar interaction
BGLU214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

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PDB entries from 2025-12-24

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