Q9NWY4: Histone PARylation factor 1 (HPF1)

Histone PARylation factor 1 (HPF1) is a 346-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NWY4.

Gene
HPF1
Organism
Homo sapiens
Length
346 residues
Mean pLDDT
90.9
Model
AF-Q9NWY4-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.9 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate84%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response (PubMed:28190768, PubMed:29480802, PubMed:29954836, PubMed:32028527, PubMed:32939087, PubMed:33186521, PubMed:33589610, PubMed:33683197, PubMed:34108479, PubMed:34210965, PubMed:34486521, PubMed:34625544, PubMed:34732825, PubMed:34795260, PubMed:34874266). Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins (PubMed:28190768, PubMed:29480802,…

Subunit structure

Interacts with PARP1 (via the PARP catalytic domain) (PubMed:27067600, PubMed:32028527, PubMed:33589610). Interacts with PARP2 (via the PARP catalytic domain) (PubMed:27067600, PubMed:32028527, PubMed:32939087, PubMed:33141820, PubMed:34108479). Interacts with core nucleosomes in a PARP1- and PARP2-dependent manner (PubMed:27067600, PubMed:32939087)

Subcellular location

Chromosome, Nucleus

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6M3GX-ray1.57 ÅA=1-346
6M3IX-ray1.98 ÅA=1-346
6TX2X-ray2.09 ÅA=37-346
6TX3X-ray2.96 ÅA=37-346
6X0LEM3.9 ÅO=1-346
9MJAEM4.3 ÅB=1-346
6X0MEM6.3 ÅO/o=1-346
6X0NEM10.0 ÅO=1-346

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