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6M3I

Crystal structure of HPF1/PARP1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006974biological_processDNA damage response
A0010835biological_processregulation of protein ADP-ribosylation
A0042393molecular_functionhistone binding
A0072572molecular_functionpoly-ADP-D-ribose binding
A0090734cellular_componentsite of DNA damage
A0140768molecular_functionprotein ADP-ribosyltransferase-substrate adaptor activity
A0140861biological_processDNA repair-dependent chromatin remodeling
B0003950molecular_functionNAD+ ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue UNU B 1101
ChainResidue
BHIS862
BGLY863
BTYR896
BPHE897
BSER904
BTYR907
BGLU988

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851
ChainResidueDetails
BGLU988

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9UGN5
ChainResidueDetails
BGLY871
BARG878
BSER904
BHIS862

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8CFE2
ChainResidueDetails
ALYS19

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:30257210
ChainResidueDetails
ASER97

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS233
ALYS186

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:33589610
ChainResidueDetails
AASP235

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: ADP-ribosyltyrosine => ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30257210
ChainResidueDetails
ATYR238

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:33589610
ChainResidueDetails
AGLU240

221051

PDB entries from 2024-06-12

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