Structure of PDB 7aks Chain GGG Binding Site BS01
Receptor Information
>7aks Chain GGG (length=333) Species:
9606
(Homo sapiens) [
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SSLSRFRGCLAGALLGDCVGSFYAAHDTVDLTSVLRHVQSLEEALYYTDD
TAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVVTVFKKLL
NPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSA
QLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQS
VLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVP
TAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAGA
YYGMDQVPESWQQSCEGYEETDILAQSLHRVFQ
Ligand information
>7aks Chain HaH (length=7) Species:
9606
(Homo sapiens) [
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PAKSAPA
Receptor-Ligand Complex Structure
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PDB
7aks
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
Resolution
1.86 Å
Binding residue
(original residue number in PDB)
A41 I271 G313 D314 D316
Binding residue
(residue number reindexed from 1)
A24 I243 G285 D286 D288
Enzymatic activity
Enzyme Commision number
3.2.1.143
: poly(ADP-ribose) glycohydrolase.
3.2.2.-
3.5.1.-
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:7aks
,
PDBe:7aks
,
PDBj:7aks
PDBsum
7aks
PubMed
34321462
UniProt
Q9NX46
|ADPRS_HUMAN ADP-ribosylhydrolase ARH3 (Gene Name=ADPRS)
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