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1GXZ

crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2; Crystal form B (P212121)

Functional Information from GO Data
ChainGOidnamespacecontents
A0106274molecular_functionNAD+-protein-arginine ADP-ribosyltransferase activity
B0106274molecular_functionNAD+-protein-arginine ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BRT A1227
ChainResidue
AARG126
AGLY127
ASER147
ASER148
ASER149
APHE160
AGLN187
AHOH2194
AHOH2195

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BRT B1227
ChainResidue
BARG126
BGLY127
BSER147
BSER148
BPHE160
BGLN187
BHOH2199

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 Residues354
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 Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosylarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"12939142","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsLipidation: {"description":"GPI-anchor amidated serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1og1
ChainResidueDetails
AGLU189
AARG184
ASER147
AGLU159

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1og1
ChainResidueDetails
BGLU189
BARG184
BSER147
BGLU159

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

site_idMCSA2
Number of Residues4
DetailsM-CSA 869
ChainResidueDetails
BSER147electrostatic stabiliser
BGLU159proton shuttle (general acid/base)
BARG184covalent catalysis, proton shuttle (general acid/base)
BGLU189electrostatic stabiliser

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PDB entries from 2025-08-27

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