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7ARW

Structure of human ARH3 E41A bound to alpha-NAD+ and magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006281biological_processDNA repair
A0006287biological_processbase-excision repair, gap-filling
A0016604cellular_componentnuclear body
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0046872molecular_functionmetal ion binding
A0060546biological_processnegative regulation of necroptotic process
A0061463molecular_functionO-acetyl-ADP-ribose deacetylase activity
A0071451biological_processcellular response to superoxide
A0090734cellular_componentsite of DNA damage
A0140290biological_processpeptidyl-serine ADP-deribosylation
A0140292molecular_functionADP-ribosylserine hydrolase activity
B0000287molecular_functionmagnesium ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006281biological_processDNA repair
B0006287biological_processbase-excision repair, gap-filling
B0016604cellular_componentnuclear body
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0046872molecular_functionmetal ion binding
B0060546biological_processnegative regulation of necroptotic process
B0061463molecular_functionO-acetyl-ADP-ribose deacetylase activity
B0071451biological_processcellular response to superoxide
B0090734cellular_componentsite of DNA damage
B0140290biological_processpeptidyl-serine ADP-deribosylation
B0140292molecular_functionADP-ribosylserine hydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AALA41
BALA41

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
ATHR76
BTHR76

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870, ECO:0007744|PDB:5ZQY, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A
ChainResidueDetails
AASP77
ALYS146
AHIS182
BASP77
BLYS146
BHIS182

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:34321462, ECO:0007744|PDB:7ARW
ChainResidueDetails
AASP78
BASP78

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:29907568, ECO:0007744|PDB:6D36, ECO:0007744|PDB:6D3A
ChainResidueDetails
ALEU235
AILE271
BLEU235
BILE271

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: 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
ChainResidueDetails
AASP314
AASP316
BASP314
BASP316

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
ATHR317
BTHR317

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Glutamate flap => ECO:0000269|PubMed:29907568, ECO:0000269|PubMed:30045870
ChainResidueDetails
AALA41
BALA41

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR64
BTHR64

222415

PDB entries from 2024-07-10

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