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6O9X

Structure of human PARG complexed with JA2-4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
A0005975biological_processcarbohydrate metabolic process
A0006282biological_processregulation of DNA repair
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue M0S A 1001
ChainResidue
ATHR725
APHE900
APHE902
AHOH1223
AILE726
AGLU727
APHE738
AGLN754
ATYR792
ATYR795
AASN869
AGLY873

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:23251397
ChainResidueDetails
AASP737

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23251397
ChainResidueDetails
AGLU755
AGLU756

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23251397, ECO:0000269|PubMed:30472116
ChainResidueDetails
AILE726
AASN740
AGLN754
AASN869

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9QYM2
ChainResidueDetails
ATYR795

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER448

218853

PDB entries from 2024-04-24

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