Poly [ADP-ribose] polymerase 2 (PARP2) is a 583-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UGN5.
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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 | 63% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 18% |
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:10364231, PubMed:25043379, PubMed:27471034, PubMed:30104678, PubMed:32028527, PubMed:32939087, PubMed:34108479, PubMed:34486521, PubMed:34874266). Mediates glutamate, aspartate or serine 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 transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:25043379, PubMed:30104678, PubMed:30321391). Serine ADP-ribosylation of proteins…
Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3 (By similarity). Homo- and heterodimer with PARP1 (PubMed:20092359). Interacts (via the PARP catalytic domain) with HPF1 (PubMed:27067600, PubMed:28190768, PubMed:32028527, PubMed:32939087, PubMed:33141820, PubMed:34108479). Interacts with core nucleosomes (PubMed:32939087, PubMed:33141820)
Nucleus, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4ZZX | X-ray | 1.65 Å | A/B=223-583 |
| 5D5K | X-ray | 1.9 Å | B=1-91 |
| 3KJD | X-ray | 1.95 Å | A/B=235-579 |
| 3KCZ | X-ray | 2.0 Å | A/B=235-579 |
| 7R59 | X-ray | 2.0 Å | A=235-583 |
| 4TVJ | X-ray | 2.1 Å | A/B=235-579 |
| 8HKO | X-ray | 2.1 Å | A/B=230-581 |
| 9IM8 | X-ray | 2.1 Å | A/B=230-581 |
| 9ZQB | EM | 2.1 Å | P=90-583 |
| 4ZZY | X-ray | 2.2 Å | A=223-583 |
| 6F1K | X-ray | 2.2 Å | A=90-218 |
| 8HLJ | X-ray | 2.24 Å | A/B=230-581 |
| 9ZQC | EM | 2.37 Å | P=90-583 |
| 4PJV | X-ray | 2.5 Å | A/B=235-579 |
| 8HKN | X-ray | 2.5 Å | A/B=230-581 |
| 5DSY | X-ray | 2.7 Å | A/B/C/D=348-583 |
| 8HLQ | X-ray | 2.7 Å | A/B=230-581 |
| 6F5B | X-ray | 2.8 Å | A/B=90-218 |
| 7AEO | X-ray | 2.8 Å | A=90-583 |
| 8HKS | X-ray | 2.8 Å | A/B/C/D=230-581 |
Showing 20 of 30 experimental structures (best resolution first).
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