Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6D3A

Structure of human ARH3 D314E bound to ADP-ribose and magnesium

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	0016604	cellular_component	nuclear body
A	0016787	molecular_function	hydrolase activity
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
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	0016604	cellular_component	nuclear body
B	0016787	molecular_function	hydrolase activity
B	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
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
C	0000287	molecular_function	magnesium ion binding
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004649	molecular_function	poly(ADP-ribose) glycohydrolase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005694	cellular_component	chromosome
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006281	biological_process	DNA repair
C	0006287	biological_process	base-excision repair, gap-filling
C	0016604	cellular_component	nuclear body
C	0016787	molecular_function	hydrolase activity
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
C	0046872	molecular_function	metal ion binding
C	0060546	biological_process	negative regulation of necroptotic process
C	0061463	molecular_function	O-acetyl-ADP-ribose deacetylase activity
C	0071451	biological_process	cellular response to superoxide
C	0090734	cellular_component	site of DNA damage
C	0140290	biological_process	peptidyl-serine ADP-deribosylation
C	0140292	molecular_function	ADP-ribosylserine hydrolase activity
D	0000287	molecular_function	magnesium ion binding
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004649	molecular_function	poly(ADP-ribose) glycohydrolase activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005694	cellular_component	chromosome
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006281	biological_process	DNA repair
D	0006287	biological_process	base-excision repair, gap-filling
D	0016604	cellular_component	nuclear body
D	0016787	molecular_function	hydrolase activity
D	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
D	0046872	molecular_function	metal ion binding
D	0060546	biological_process	negative regulation of necroptotic process
D	0061463	molecular_function	O-acetyl-ADP-ribose deacetylase activity
D	0071451	biological_process	cellular response to superoxide
D	0090734	cellular_component	site of DNA damage
D	0140290	biological_process	peptidyl-serine ADP-deribosylation
D	0140292	molecular_function	ADP-ribosylserine hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue AR6 C 401

Chain	Residue
C	ASP77
C	GLY150
C	ASN151
C	GLY152
C	HIS182
C	ILE271
C	GLU314
C	THR317
C	MG402
C	HOH504
C	HOH538
C	GLY115
C	HOH550
C	HOH553
C	HOH566
C	GLY117
C	GLY119
C	VAL120
C	PHE143
C	GLY147
C	SER148
C	TYR149

site_id	AC2
Number of Residues	7
Details	binding site for residue MG C 402

Chain	Residue
C	THR76
C	ASP77
C	ASP78
C	ASP316
C	AR6401
C	HOH504
C	HOH602

site_id	AC3
Number of Residues	23
Details	binding site for residue AR6 D 401

Chain	Residue
D	ASP77
D	GLY115
D	GLY117
D	GLY119
D	VAL120
D	PHE143
D	GLY147
D	SER148
D	TYR149
D	GLY150
D	ASN151
D	GLY152
D	HIS182
D	LEU235
D	ILE271
D	GLU314
D	THR317
D	MG402
D	HOH502
D	HOH534
D	HOH536
D	HOH541
D	HOH582

site_id	AC4
Number of Residues	7
Details	binding site for residue MG D 402

Chain	Residue
D	THR76
D	ASP77
D	ASP78
D	ASP316
D	AR6401
D	HOH502
D	HOH697

site_id	AC5
Number of Residues	24
Details	binding site for residue AR6 A 401

Chain	Residue
A	ASP77
A	GLY115
A	TYR116
A	GLY117
A	ALA118
A	GLY119
A	VAL120
A	PHE143
A	GLY147
A	SER148
A	TYR149
A	GLY150
A	ASN151
A	GLY152
A	HIS182
A	ILE271
A	GLU314
A	MG402
A	HOH526
A	HOH539
A	HOH550
A	HOH565
A	HOH567
A	HOH598

site_id	AC6
Number of Residues	7
Details	binding site for residue MG A 402

Chain	Residue
A	THR76
A	ASP77
A	ASP78
A	ASP316
A	AR6401
A	HOH550
A	HOH645

site_id	AC7
Number of Residues	24
Details	binding site for residue AR6 B 401

Chain	Residue
B	TYR149
B	GLY150
B	ASN151
B	GLY152
B	HIS182
B	ILE271
B	GLU314
B	THR317
B	MG402
B	HOH503
B	HOH529
B	HOH531
B	HOH534
B	HOH560
B	HOH595
B	ASP77
B	GLY115
B	GLY117
B	GLY119
B	VAL120
B	PHE143
B	LYS146
B	GLY147
B	SER148

site_id	AC8
Number of Residues	7
Details	binding site for residue MG B 402

Chain	Residue
B	THR76
B	ASP77
B	ASP78
B	ASP316
B	AR6401
B	HOH503
B	HOH554

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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
C	GLU41
D	GLU41
A	GLU41
B	GLU41

site_id	SWS_FT_FI2
Number of Residues	4
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
C	THR76
D	THR76
A	THR76
B	THR76

site_id	SWS_FT_FI3
Number of Residues	12
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
C	ASP77
B	ASP77
B	LYS146
B	HIS182
C	LYS146
C	HIS182
D	ASP77
D	LYS146
D	HIS182
A	ASP77
A	LYS146
A	HIS182

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:34321462, ECO:0007744\|PDB:7ARW

Chain	Residue	Details
C	ASP78
D	ASP78
A	ASP78
B	ASP78

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:29907568, ECO:0007744\|PDB:6D36, ECO:0007744\|PDB:6D3A

Chain	Residue	Details
C	LEU235
C	ILE271
D	LEU235
D	ILE271
A	LEU235
A	ILE271
B	LEU235
B	ILE271

site_id	SWS_FT_FI6
Number of Residues	8
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
C	GLU314
C	ASP316
D	GLU314
D	ASP316
A	GLU314
A	ASP316
B	GLU314
B	ASP316

site_id	SWS_FT_FI7
Number of Residues	4
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
C	THR317
D	THR317
A	THR317
B	THR317

site_id	SWS_FT_FI8
Number of Residues	4
Details	SITE: Glutamate flap => ECO:0000269\|PubMed:29907568, ECO:0000269\|PubMed:30045870

Chain	Residue	Details
C	GLU41
D	GLU41
A	GLU41
B	GLU41

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	THR64
D	THR64
A	THR64
B	THR64

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