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1OG3

Crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2 mutant E189I in complex with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0106274molecular_functionNAD+-protein-arginine ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD A1227
ChainResidue
ALEU5
AGLN144
ASER147
APHE160
AGLN187
AILE189
AHOH2056
AHOH2057
AHOH2058
AHOH2065
AHOH2068
ALYS65
AHOH2069
AHOH2099
AHOH2120
AHOH2126
AHOH2149
AHOH2150
AHOH2151
AHOH2152
AHOH2153
AHOH2154
AVAL84
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 Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340
ChainResidueDetails
AARG126
ASER147
AILE189

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ATYR78
AARG126
AGLN144
ASER182

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by autocatalysis => ECO:0000305|PubMed:12939142
ChainResidueDetails
AARG184

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: GPI-anchor amidated serine => ECO:0000250
ChainResidueDetails
ASER226

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1og1
ChainResidueDetails
AILE189
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)
AILE189electrostatic stabiliser

224004

PDB entries from 2024-08-21

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