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6TX3

HPF1 bound to catalytic fragment of PARP2

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 Residues14
Detailsbinding site for residue UHB B 1001
ChainResidue
BHIS415
BTYR442
BTYR449
BSER457
BTYR460
BGLU545
BGLY416
BSER417
BASN421
BGLY424
BILE425
BGLY429
BARG431
BPRO434

Functional Information from PROSITE/UniProt
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANPKA
ChainResidueDetails
BLEU485-ALA492

site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HgsrmSnwVgILSHG
ChainResidueDetails
BHIS415-GLY429

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:32028527, ECO:0000269|PubMed:33589610, ECO:0000269|PubMed:33683197
ChainResidueDetails
AGLU284

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:30257210
ChainResidueDetails
ASER97
BGLY424
BARG431
BSER457

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS186
ALYS233

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl aspartic acid => ECO:0000269|PubMed:33589610
ChainResidueDetails
AASP235

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: ADP-ribosyltyrosine => ECO:0000269|PubMed:29954836, ECO:0000269|PubMed:30257210
ChainResidueDetails
ATYR238

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:33589610
ChainResidueDetails
AGLU240

222415

PDB entries from 2024-07-10

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