1GY0

crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM C (P3121)

Functional Information from GO Data

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

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	177
Details	Domain: {"description":"TR mART core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01340","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylarginine; by autocatalysis","evidences":[{"source":"PubMed","id":"12939142","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Lipidation: {"description":"GPI-anchor amidated serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1og1

Chain	Residue	Details
A	GLU189
A	ARG184
A	SER147
A	GLU159

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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	GLU189	electrostatic stabiliser

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