Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FP0

human ADP-ribosylhydrolase 3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004649	molecular_function	poly(ADP-ribose) glycohydrolase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006281	biological_process	DNA repair
A	0006287	biological_process	base-excision repair, gap-filling
A	0006974	biological_process	DNA damage response
A	0016604	cellular_component	nuclear body
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0060546	biological_process	negative regulation of necroptotic process
A	0061463	molecular_function	O-acetyl-ADP-ribose deacetylase activity
A	0071451	biological_process	cellular response to superoxide
A	0090734	cellular_component	site of DNA damage
A	0140290	biological_process	peptidyl-serine ADP-deribosylation
A	0140292	molecular_function	ADP-ribosylserine hydrolase activity
B	0000287	molecular_function	magnesium ion binding
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004649	molecular_function	poly(ADP-ribose) glycohydrolase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005694	cellular_component	chromosome
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006281	biological_process	DNA repair
B	0006287	biological_process	base-excision repair, gap-filling
B	0006974	biological_process	DNA damage response
B	0016604	cellular_component	nuclear body
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0060546	biological_process	negative regulation of necroptotic process
B	0061463	molecular_function	O-acetyl-ADP-ribose deacetylase activity
B	0071451	biological_process	cellular response to superoxide
B	0090734	cellular_component	site of DNA damage
B	0140290	biological_process	peptidyl-serine ADP-deribosylation
B	0140292	molecular_function	ADP-ribosylserine hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	THR60
A	ASP61
A	ASP62
A	ASP300
A	HOH403
A	HOH405
A	HOH406
A	HOH407

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 402

Chain	Residue
A	ASP300
A	THR301
A	HOH403
A	HOH404
A	HOH407
A	ASP298

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	THR60
B	ASP61
B	ASP62
B	ASP300
B	HOH527
B	HOH528
B	HOH529
B	HOH531

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	ASP298
B	ASP300
B	THR301
B	HOH527
B	HOH528
B	HOH530

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21892188, ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870, ECO:0007744\|PDB:5ZQY, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A

Chain	Residue	Details
A	GLU25
B	GLU25

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21892188, ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870, ECO:0000269\|PubMed:33894202, ECO:0007744\|PDB:5ZQY, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A, ECO:0007744\|PDB:7L9I

Chain	Residue	Details
A	THR60
B	THR60

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870, ECO:0007744\|PDB:5ZQY, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A

Chain	Residue	Details
A	ASP61
A	LYS130
A	HIS166
B	ASP61
B	LYS130
B	HIS166

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:34321462, ECO:0007744\|PDB:7ARW

Chain	Residue	Details
A	ASP62
B	ASP62

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:29907568, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A

Chain	Residue	Details
A	LEU219
A	ILE255
B	LEU219
B	ILE255

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:21892188, ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870, ECO:0000269\|PubMed:33894202, ECO:0000269\|PubMed:34321462, ECO:0007744\|PDB:5ZQY, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A, ECO:0007744\|PDB:7AKR, ECO:0007744\|PDB:7AKS, ECO:0007744\|PDB:7ARW, ECO:0007744\|PDB:7L9H

Chain	Residue	Details
A	ASP298
A	ASP300
B	ASP298
B	ASP300

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21892188, ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870, ECO:0000269\|PubMed:33894202, ECO:0007744\|PDB:5ZQY, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A, ECO:0007744\|PDB:7L9H

Chain	Residue	Details
A	THR301
B	THR301

site_id	SWS_FT_FI8
Number of Residues	2
Details	SITE: Glutamate flap => ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870

Chain	Residue	Details
A	GLU25
B	GLU25

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR48
B	THR48

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)