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6X0M

Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin

Functional Information from GO Data
ChainGOidnamespacecontents
O0000785cellular_componentchromatin
O0003682molecular_functionchromatin binding
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005694cellular_componentchromosome
O0006281biological_processDNA repair
O0006302biological_processdouble-strand break repair
O0006974biological_processDNA damage response
O0010835biological_processregulation of protein ADP-ribosylation
O0042393molecular_functionhistone binding
O0070212biological_processprotein poly-ADP-ribosylation
O0071168biological_processprotein localization to chromatin
O0072572molecular_functionpoly-ADP-D-ribose binding
O0090734cellular_componentsite of DNA damage
O0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
O0140861biological_processDNA repair-dependent chromatin remodeling
P0003677molecular_functionDNA binding
P0003682molecular_functionchromatin binding
P0003684molecular_functiondamaged DNA binding
P0003824molecular_functioncatalytic activity
P0003950molecular_functionNAD+ poly-ADP-ribosyltransferase activity
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0005654cellular_componentnucleoplasm
P0005694cellular_componentchromosome
P0005730cellular_componentnucleolus
P0005829cellular_componentcytosol
P0006281biological_processDNA repair
P0006284biological_processbase-excision repair
P0006302biological_processdouble-strand break repair
P0006974biological_processDNA damage response
P0016740molecular_functiontransferase activity
P0016757molecular_functionglycosyltransferase activity
P0016779molecular_functionnucleotidyltransferase activity
P0030592biological_processDNA ADP-ribosylation
P0031491molecular_functionnucleosome binding
P0046697biological_processdecidualization
P0061051biological_processpositive regulation of cell growth involved in cardiac muscle cell development
P0070212biological_processprotein poly-ADP-ribosylation
P0070213biological_processprotein auto-ADP-ribosylation
P0071168biological_processprotein localization to chromatin
P0072572molecular_functionpoly-ADP-D-ribose binding
P0090649biological_processresponse to oxygen-glucose deprivation
P0090734cellular_componentsite of DNA damage
P0097191biological_processextrinsic apoptotic signaling pathway
P0110088biological_processhippocampal neuron apoptotic process
P0140294molecular_functionNAD DNA ADP-ribosyltransferase activity
P0140805molecular_functionNAD+-protein-serine ADP-ribosyltransferase activity
P0140806molecular_functionNAD+-protein-aspartate ADP-ribosyltransferase activity
P0140807molecular_functionNAD+-protein-glutamate ADP-ribosyltransferase activity
P0140861biological_processDNA repair-dependent chromatin remodeling
P0160004molecular_functionpoly-ADP-D-ribose modification-dependent protein binding
P1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
o0000785cellular_componentchromatin
o0003682molecular_functionchromatin binding
o0005515molecular_functionprotein binding
o0005634cellular_componentnucleus
o0005694cellular_componentchromosome
o0006281biological_processDNA repair
o0006302biological_processdouble-strand break repair
o0006974biological_processDNA damage response
o0010835biological_processregulation of protein ADP-ribosylation
o0042393molecular_functionhistone binding
o0070212biological_processprotein poly-ADP-ribosylation
o0071168biological_processprotein localization to chromatin
o0072572molecular_functionpoly-ADP-D-ribose binding
o0090734cellular_componentsite of DNA damage
o0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
o0140861biological_processDNA repair-dependent chromatin remodeling
p0003677molecular_functionDNA binding
p0003682molecular_functionchromatin binding
p0003684molecular_functiondamaged DNA binding
p0003824molecular_functioncatalytic activity
p0003950molecular_functionNAD+ poly-ADP-ribosyltransferase activity
p0005515molecular_functionprotein binding
p0005634cellular_componentnucleus
p0005654cellular_componentnucleoplasm
p0005694cellular_componentchromosome
p0005730cellular_componentnucleolus
p0005829cellular_componentcytosol
p0006281biological_processDNA repair
p0006284biological_processbase-excision repair
p0006302biological_processdouble-strand break repair
p0006974biological_processDNA damage response
p0016740molecular_functiontransferase activity
p0016757molecular_functionglycosyltransferase activity
p0016779molecular_functionnucleotidyltransferase activity
p0030592biological_processDNA ADP-ribosylation
p0031491molecular_functionnucleosome binding
p0046697biological_processdecidualization
p0061051biological_processpositive regulation of cell growth involved in cardiac muscle cell development
p0070212biological_processprotein poly-ADP-ribosylation
p0070213biological_processprotein auto-ADP-ribosylation
p0071168biological_processprotein localization to chromatin
p0072572molecular_functionpoly-ADP-D-ribose binding
p0090649biological_processresponse to oxygen-glucose deprivation
p0090734cellular_componentsite of DNA damage
p0097191biological_processextrinsic apoptotic signaling pathway
p0110088biological_processhippocampal neuron apoptotic process
p0140294molecular_functionNAD DNA ADP-ribosyltransferase activity
p0140805molecular_functionNAD+-protein-serine ADP-ribosyltransferase activity
p0140806molecular_functionNAD+-protein-aspartate ADP-ribosyltransferase activity
p0140807molecular_functionNAD+-protein-glutamate ADP-ribosyltransferase activity
p0140861biological_processDNA repair-dependent chromatin remodeling
p0160004molecular_functionpoly-ADP-D-ribose modification-dependent protein binding
p1990404molecular_functionNAD+-protein mono-ADP-ribosyltransferase activity
Functional Information from PROSITE/UniProt
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANPKA
ChainResidueDetails
PLEU485-ALA492

site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HgsrmSnwVgILSHG
ChainResidueDetails
PHIS415-GLY429

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33683197","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"PolyADP-ribosyl aspartic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosyltyrosine","evidences":[{"source":"PubMed","id":"29954836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30257210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues194
DetailsDomain: {"description":"WGR","evidences":[{"source":"PROSITE-ProRule","id":"PRU01321","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues454
DetailsDomain: {"description":"PARP catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00397","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"description":"For poly [ADP-ribose] polymerase activity","evidences":[{"source":"PubMed","id":"26704974","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30104678","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TX3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsSite: {"description":"Cleavage; by caspase-8","evidences":[{"source":"UniProtKB","id":"O88554","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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