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1GXY

crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM A (P21)

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 Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1227
ChainResidue
AARG126
AGLY127
ASER147
ASER148
AALA155
APHE160
AHOH2254
AHOH2255

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 1227
ChainResidue
BGLY127
BSER147
BSER148
BALA155
BPHE160
BGLN187
BGLU189
BHOH2242
BHOH2243
BARG126

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 Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340
ChainResidueDetails
AARG126
ASER147
AGLU189
BARG126
BSER147
BGLU189

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ATYR78
AARG126
AGLN144
ASER182
BTYR78
BARG126
BGLN144
BSER182

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by autocatalysis => ECO:0000305|PubMed:12939142
ChainResidueDetails
AARG184
BARG184

site_idSWS_FT_FI4
Number of Residues2
DetailsLIPID: GPI-anchor amidated serine => ECO:0000250
ChainResidueDetails
ASER226
BSER226

Catalytic Information from CSA
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 2024-04-24

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