2QTY

Crystal Structure of mouse ADP-ribosylhydrolase 3 (mARH3)

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	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	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	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	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	6
Details	BINDING SITE FOR RESIDUE MG A 348

Chain	Residue
A	THR60
A	ASP61
A	ASP62
A	ASP300
A	HOH359
A	HOH382

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 349

Chain	Residue
A	THR301
A	HOH371
A	HOH382
A	GLU25
A	ASP298
A	ASP300

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 348

Chain	Residue
B	THR60
B	ASP61
B	ASP62
B	ASP300
B	HOH367
B	HOH371

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 349

Chain	Residue
B	GLU25
B	ASP298
B	ASP300
B	THR301
B	HOH367
B	HOH423

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:18323597

Chain	Residue	Details
A	GLU25
B	ASP298
B	ASP300
B	THR301
A	THR60
A	ASP62
A	ASP298
A	ASP300
A	THR301
B	GLU25
B	THR60
B	ASP62

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9NX46

Chain	Residue	Details
A	ASP61
B	ILE255
A	LYS130
A	HIS166
A	LEU219
A	ILE255
B	ASP61
B	LYS130
B	HIS166
B	LEU219

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Glutamate flap => ECO:0000250|UniProtKB:Q9NX46

Chain	Residue	Details
A	GLU25
B	GLU25

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9NX46

Chain	Residue	Details
A	THR48
B	THR48

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