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4EPQ

canonical poly(ADP-ribose) glycohydrolase RBPI inhibitor complex from Tetrahymena thermophila

Functional Information from GO Data
ChainGOidnamespacecontents
A0004649molecular_functionpoly(ADP-ribose) glycohydrolase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006282biological_processregulation of DNA repair
A0009225biological_processnucleotide-sugar metabolic process
A0016787molecular_functionhydrolase activity
A0072570molecular_functionADP-D-ribose binding
A0140292molecular_functionADP-ribosylserine hydrolase activity
A1990966biological_processATP generation from poly-ADP-D-ribose
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0RR A 501
ChainResidue
APHE238
APHE398
AGLN399
AHOH645
AGLN254
ATYR293
AGLY295
ATYR296
ALYS365
AGLY367
ACYS368
AGLY369

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues117
DetailsDomain: {"description":"PARG helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues191
DetailsDomain: {"description":"PARG catalytic Macro","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22673905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EPP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L2H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Sterically interferes with binding of internal ADP-D-ribose moieties of poly(ADP-ribose) to preferentially bind terminal moieties and drive exo-glycohydrolitic activity","evidences":[{"source":"PubMed","id":"23917065","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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