Poly [ADP-ribose] polymerase 1 (PARP1) is a 1014-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09874.
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The mean pLDDT of this model is 82.4 (confident 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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 50% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18055453, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:20388712, PubMed:21680843, PubMed:22582261, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:26626479, PubMed:26626480, PubMed:30104678, PubMed:31796734, PubMed:32028527, PubMed:32241924, PubMed:32358582, PubMed:33186521, PubMed:34465625, PubMed:34737271). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are…
Homodimer; PARP-type zinc-fingers from separate PARP1 molecules form a dimer module that specifically recognizes DNA strand breaks (PubMed:22683995). Heterodimer; heterodimerizes with PARP2 (By similarity). Interacts (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33589610). Interacts with NMNAT1 (By similarity). Interacts…
Chromosome, Nucleus, Nucleus, nucleolus, Cytoplasm, cytosol, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6NRH | X-ray | 1.5 Å | A=788-1012 |
| 7AAC | X-ray | 1.59 Å | A/B=662-1011 |
| 9ETQ | X-ray | 1.59 Å | A/B=662-1011 |
| 6NRJ | X-ray | 1.65 Å | A=788-1012 |
| 2RIQ | X-ray | 1.7 Å | A=216-366 |
| 6NRG | X-ray | 1.7 Å | A=788-1012 |
| 7KK2 | X-ray | 1.7 Å | A/B=662-1011 |
| 7KK5 | X-ray | 1.7 Å | A/B/C/D=662-1011 |
| 7AAA | X-ray | 1.74 Å | A/B=662-1011 |
| 6NTU | X-ray | 1.8 Å | A=788-1012 |
| 9ETR | X-ray | 1.82 Å | A/B=662-1011 |
| 7ONT | X-ray | 1.85 Å | A/B=662-1011 |
| 4ZZZ | X-ray | 1.9 Å | A/B=655-1014 |
| 5WS1 | X-ray | 1.9 Å | A/B=662-1011 |
| 7KK4 | X-ray | 1.96 Å | A/B=662-1011 |
| 7ONS | X-ray | 1.97 Å | A/B=662-1011 |
| 6M3I | X-ray | 1.98 Å | B=788-1014 |
| 6NRF | X-ray | 2.0 Å | A=788-1012 |
| 6XVW | X-ray | 2.0 Å | A/B=663-1014 |
| 7ONR | X-ray | 2.05 Å | A/B=662-1011 |
Showing 20 of 106 experimental structures (best resolution first).
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