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2C8C

Structure of the ARTT motif Q212A mutant C3bot1 Exoenzyme (NAD-bound state, crystal form I)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016763molecular_functionpentosyltransferase activity
A1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
B0005576cellular_componentextracellular region
B0016763molecular_functionpentosyltransferase activity
B1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
C0005576cellular_componentextracellular region
C0016763molecular_functionpentosyltransferase activity
C1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
D0005576cellular_componentextracellular region
D0016763molecular_functionpentosyltransferase activity
D1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAD A 1248
ChainResidue
ATHR80
AGLU169
ATHR175
ASER176
APHE183
AARG186
AGLU214
AASN87
AARG91
AARG128
AGLY129
AASP130
AASP131
AALA133
AARG167

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD B 1248
ChainResidue
BSER84
BASN87
BARG91
BARG128
BGLY129
BASP130
BASP131
BALA133
BARG167
BGLU169
BSER174
BPHE183
BARG186
BPHE209
BGLY211
BGLU214

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAD C 1252
ChainResidue
CSER84
CASN87
CARG91
CARG128
CGLY129
CASP130
CASP131
CALA133
CTYR134
CARG167
CGLU169
CTHR175
CSER176
CPHE183
CARG186
CGLU214

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ADP D 1247
ChainResidue
DASN87
DARG91
DARG128
DASP130
DASP131
DALA133
DARG167
DGLU169
DARG186

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
DetailsAnnotated By Reference To The Literature 1g24
ChainResidueDetails
AGLU214

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

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g24
ChainResidueDetails
CGLU214

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g24
ChainResidueDetails
DGLU214

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

site_idMCSA3
Number of Residues2
DetailsM-CSA 824
ChainResidueDetails
CSER174electrostatic stabiliser, polar interaction
CGLU214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

site_idMCSA4
Number of Residues2
DetailsM-CSA 824
ChainResidueDetails
DSER174electrostatic stabiliser, polar interaction
DGLU214electrostatic stabiliser, polar interaction, proton acceptor, proton donor

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PDB entries from 2025-07-23

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