4ZZY

Structure of human PARP2 catalytic domain bound to an isoindolinone inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003950	molecular_function	NAD+ poly-ADP-ribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE D7N A 1584

Chain	Residue
A	SER328
A	ALA464
A	LYS469
A	SER470
A	TYR473
A	GLU558
A	ILE331
A	GLN332
A	HIS428
A	GLY429
A	GLY454
A	TYR455
A	TYR462
A	PHE463

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Functional Information from PROSITE/UniProt

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANPKA

Chain	Residue	Details
A	LEU498-ALA505

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site_id	PS01121
Number of Residues	15
Details	CASPASE_HIS Caspase family histidine active site. HgsrmSnwVgILSHG

Chain	Residue	Details
A	HIS428-GLY442

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	117
Details	Domain: {"description":"PARP alpha-helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00398","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"For poly [ADP-ribose] polymerase activity","evidences":[{"source":"PubMed","id":"26704974","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30104678","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TX3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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