Structure of PDB 2qty Chain A

Receptor sequence
>2qtyA (length=337) Species: 10090 (Mus musculus) [Search protein sequence]
MASISRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESLEPETLYYT
DDTAMTRALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFKK
LLNPKCRDVYEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARL
SAQLTHASSLGYNGAILQALAVHLALQGVSSSEHFLEQLLGHMEELEGDA
QSVLDAKELGMEERPYSSRLKKVGELLDQDVVSREEVVSELGNGIAAFES
VPTAIYCFLRCMEPHPEIPSTFNSLQRTLIYSISLGGDTDTIATMAGAIA
GAYYGMEQVPESWQQSCEGFEETDVLAQSLHRVFQES
3D structure
PDB2qty Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
ChainA
Resolution1.8 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 MG A T60 D61 D62 D300 T50 D51 D52 D290
BS02 MG A E25 D298 D300 T301 E25 D288 D290 T291
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: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: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:2qty, PDBe:2qty, PDBj:2qty
PDBsum2qty
PubMed18323597
UniProtQ8CG72|ADPRS_MOUSE ADP-ribosylhydrolase ARH3 (Gene Name=Adprs)

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