1OG4

Crystal Structure of the Eucaryotic Mono-ADP-Ribosyltransferase ART2.2 Mutant E189A in Complex with NADH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0106274	molecular_function	NAD+-protein-arginine ADP-ribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAI A1227

Chain	Residue
A	LEU5
A	SER148
A	ALA155
A	PHE160
A	GLN187
A	HOH2068
A	HOH2095
A	HOH2134
A	HOH2135
A	HOH2136
A	HOH2137
A	THR79
A	HOH2138
A	ASN87
A	ARG91
A	ARG126
A	GLY127
A	PHE132
A	GLN144
A	SER147

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Functional Information from PROSITE/UniProt

site_id	PS01291
Number of Residues	13
Details	ART NAD:arginine ADP-ribosyltransferases signature. FhYKafHYyLTrA

Chain	Residue	Details
A	PHE100-ALA112

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340

Chain	Residue	Details
A	ARG126
A	SER147
A	ALA189

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	TYR78
A	ARG126
A	GLN144
A	SER182

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by autocatalysis => ECO:0000305|PubMed:12939142

Chain	Residue	Details
A	ARG184

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site_id	SWS_FT_FI4
Number of Residues	1
Details	LIPID: GPI-anchor amidated serine => ECO:0000250

Chain	Residue	Details
A	SER226

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 869

Chain	Residue	Details
A	SER147	electrostatic stabiliser
A	GLU159	proton shuttle (general acid/base)
A	ARG184	covalent catalysis, proton shuttle (general acid/base)
A	ALA189	electrostatic stabiliser

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