Structure of PDB 7l9h Chain C

Receptor sequence
>7l9hC (length=336) Species: 9606 (Homo sapiens) [Search protein sequence]
AGAARSLSRFRGCLAGALLGDCVGSFYEVDLTSVLRHVQSLETEALYYTA
DTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVVTVFKKL
LNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLS
AQLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQ
SVLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESV
PTAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAG
AYYGMDQVPESWQQSCEGYEETDILAQSLHRVFQKS
3D structure
PDB7l9h Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.
ChainC
Resolution1.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.143: poly(ADP-ribose) glycohydrolase.
3.2.2.-
3.5.1.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AR6 C D78 G115 G117 G119 V120 F143 S148 Y149 G150 N151 G152 H182 D314 D316 T317 D51 G88 G90 G92 V93 F116 S121 Y122 G123 N124 G125 H155 D287 D289 T290
BS02 MG C D314 D316 T317 D287 D289 T290
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004649 poly(ADP-ribose) glycohydrolase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0046872 metal ion binding
GO:0061463 O-acetyl-ADP-ribose deacetylase activity
GO:0140292 ADP-ribosylserine hydrolase activity
Biological Process
GO:0006281 DNA repair
GO:0006287 base-excision repair, gap-filling
GO:0060546 negative regulation of necroptotic process
GO:0071451 cellular response to superoxide
GO:0140290 peptidyl-serine ADP-deribosylation
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0016604 nuclear body
GO:0090734 site of DNA damage

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7l9h, PDBe:7l9h, PDBj:7l9h
PDBsum7l9h
PubMed33894202
UniProtQ9NX46|ADPRS_HUMAN ADP-ribosylhydrolase ARH3 (Gene Name=ADPRS)

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