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1OG1

CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 IN COMPLEX WITH TAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0106274molecular_functionNAD+-protein-arginine ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE TAD A1227
ChainResidue
ALEU5
AGLN144
ASER147
APHE160
AGLU189
AHOH2030
AHOH2067
AHOH2077
AHOH2079
AHOH2091
AHOH2127
ALYS65
AHOH2176
AHOH2177
AHOH2178
AHOH2179
ATHR79
AASN87
AARG91
AARG126
AGLY127
ATHR130
APHE132

Functional Information from PROSITE/UniProt
site_idPS01291
Number of Residues13
DetailsART NAD:arginine ADP-ribosyltransferases signature. FhYKafHYyLTrA
ChainResidueDetails
APHE100-ALA112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues177
DetailsDomain: {"description":"TR mART core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"12939142","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsLipidation: {"description":"GPI-anchor amidated serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 12939142
ChainResidueDetails
AGLU189
AARG184
ASER147
AGLU159

site_idMCSA1
Number of Residues4
DetailsM-CSA 869
ChainResidueDetails
ASER147electrostatic stabiliser
AGLU159proton shuttle (general acid/base)
AARG184covalent catalysis, proton shuttle (general acid/base)
AGLU189electrostatic stabiliser

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PDB entries from 2026-01-14

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