Replication protein A 32 kDa subunit (RPA2) is a 270-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15927.
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The mean pLDDT of this model is 79.3 (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 | 56% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 22% |
What pLDDT means and how to read it
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break…
Component of the replication protein A complex (RPA/RP-A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3 (PubMed:10449415, PubMed:19116208, PubMed:2406247). Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA) (PubMed:24332808). Interacts with SERTAD3 (PubMed:10982866). Interacts with…
Nucleus, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4OU0 | X-ray | 1.4 Å | A=202-270 |
| 4MQV | X-ray | 1.95 Å | A/C=202-270 |
| 3KDF | X-ray | 1.98 Å | B/D=41-172 |
| 2PI2 | X-ray | 2.0 Å | A/B/C/D=1-270 |
| 1QUQ | X-ray | 2.5 Å | A/C=43-171 |
| 2PQA | X-ray | 2.5 Å | A/C=42-172 |
| 1L1O | X-ray | 2.8 Å | B/E=44-171 |
| 2Z6K | X-ray | 3.0 Å | A/B=1-270 |
| 8RK2 | EM | 3.2 Å | B=1-270 |
| 9PD3 | EM | 3.3 Å | O=1-270 |
| 9PD4 | EM | 3.4 Å | O=1-270 |
| 9MJ5 | EM | 3.5 Å | B=35-270 |
| 1DPU | NMR | A=172-270 | |
| 1Z1D | NMR | A=172-270 |
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