Replication protein A 70 kDa DNA-binding subunit (RPA1) is a 616-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P27694.
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The mean pLDDT of this model is 83.8 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 12% |
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 (PubMed:17596542, PubMed:27723717, PubMed:27723720). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). 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…
Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3 (PubMed:27723717, PubMed:27723720, PubMed:34767620). Also a component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2 (PubMed:19116208,…
Nucleus, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4O0A | X-ray | 1.2 Å | A=1-120 |
| 5E7N | X-ray | 1.21 Å | A=1-120 |
| 4IPC | X-ray | 1.22 Å | A=1-120 |
| 4R4T | X-ray | 1.28 Å | A=1-120 |
| 5N8A | X-ray | 1.28 Å | A=1-120 |
| 4R4O | X-ray | 1.33 Å | A=1-120 |
| 4NB3 | X-ray | 1.35 Å | A/B=1-120 |
| 4R4Q | X-ray | 1.35 Å | A=1-120 |
| 4LUV | X-ray | 1.4 Å | A=1-120 |
| 4R4C | X-ray | 1.4 Å | A=1-120 |
| 4R4I | X-ray | 1.4 Å | A=1-120 |
| 8K00 | X-ray | 1.4 Å | A=1-120 |
| 4IJH | X-ray | 1.5 Å | A=1-120 |
| 7XV0 | X-ray | 1.5 Å | A=1-121 |
| 8JZV | X-ray | 1.5 Å | A=1-120 |
| 8JZY | X-ray | 1.5 Å | A=1-120 |
| 4IPD | X-ray | 1.51 Å | A=1-120 |
| 4LUO | X-ray | 1.54 Å | A=1-120 |
| 5EAY | X-ray | 1.55 Å | A/B/C/D=3-120 |
| 9J1S | X-ray | 1.55 Å | A=1-120 |
Showing 20 of 42 experimental structures (best resolution first).
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