Structure of PDB 6x0m Chain p

Receptor sequence
>6x0mp (length=468) Species: 9606 (Homo sapiens) [Search protein sequence]
APVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDA
QRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDR
EKFEKVPGKYDMLQMDYQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKA
PLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGL
RTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNL
HCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEA
FREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFAD
MSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHST
KGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPN
QVRMRYLLKVQFNFLQLW
3D structure
PDB6x0m Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin.
Chainp
Resolution6.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S457 Y460 E545
Catalytic site (residue number reindexed from 1) S355 Y358 E443
Enzyme Commision number 2.4.2.-
2.4.2.30: NAD(+) ADP-ribosyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 dna p Y119 W138 K170 Y188 Y41 W60 K92 Y110
BS02 dna p N114 N115 N116 K117 G139 R140 Q146 N36 N37 N38 K39 G61 R62 Q68
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003682 chromatin binding
GO:0003684 damaged DNA binding
GO:0003950 NAD+-protein poly-ADP-ribosyltransferase activity
GO:0005515 protein binding
GO:0016757 glycosyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0031491 nucleosome binding
GO:0072572 poly-ADP-D-ribose binding
GO:0140294 NAD DNA ADP-ribosyltransferase activity
GO:0140805 NAD+-protein-serine ADP-ribosyltransferase activity
GO:0140806 NAD+-protein-aspartate ADP-ribosyltransferase activity
GO:0140807 NAD+-protein-glutamate ADP-ribosyltransferase activity
GO:0160004 poly-ADP-D-ribose modification-dependent protein binding
GO:1990404 NAD+-protein ADP-ribosyltransferase activity
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006302 double-strand break repair
GO:0006974 DNA damage response
GO:0030592 DNA ADP-ribosylation
GO:0046697 decidualization
GO:0061051 positive regulation of cell growth involved in cardiac muscle cell development
GO:0070212 protein poly-ADP-ribosylation
GO:0070213 protein auto-ADP-ribosylation
GO:0090649 response to oxygen-glucose deprivation
GO:0097191 extrinsic apoptotic signaling pathway
GO:0110088 hippocampal neuron apoptotic process
GO:0140861 DNA repair-dependent chromatin remodeling
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005694 chromosome
GO:0005730 nucleolus
GO:0090734 site of DNA damage

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6x0m, PDBe:6x0m, PDBj:6x0m
PDBsum6x0m
PubMed32939087
UniProtQ9UGN5|PARP2_HUMAN Poly [ADP-ribose] polymerase 2 (Gene Name=PARP2)

[Back to BioLiP]