Replication factor C subunit 1 (RFC1) is a 861-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P38630.
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The mean pLDDT of this model is 71.4 (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 | 26% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Component of the ATP-dependent clamp loader RFC complex for the POL30/PCNA homotrimer DNA clamp. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Replication factor C (RFC or activator 1) complex acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion…
Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Interacts with ECO1 and POL30/PCNA
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8DQX | EM | 2.1 Å | A=1-861 |
| 8DR1 | EM | 2.14 Å | A=1-861 |
| 8DR3 | EM | 2.2 Å | A=1-861 |
| 8DR6 | EM | 2.39 Å | A=1-861 |
| 8DR0 | EM | 2.42 Å | A=1-861 |
| 8DR4 | EM | 2.45 Å | A=1-861 |
| 9PEO | EM | 2.57 Å | A=1-861 |
| 9PER | EM | 2.57 Å | A=1-861 |
| 9PET | EM | 2.57 Å | A=1-861 |
| 9PES | EM | 2.59 Å | A=1-861 |
| 9PEU | EM | 2.62 Å | A=1-861 |
| 9PEV | EM | 2.63 Å | A=1-861 |
| 8DR7 | EM | 2.7 Å | A=1-861 |
| 8DR5 | EM | 2.76 Å | A=1-861 |
| 1SXJ | X-ray | 2.85 Å | A=295-785 |
| 8DQZ | EM | 2.92 Å | A=1-861 |
| 7U1P | EM | 3.0 Å | A=1-861 |
| 7TFH | EM | 3.09 Å | A=1-861 |
| 7TFK | EM | 3.25 Å | A=1-861 |
| 7TFJ | EM | 3.3 Å | A=1-861 |
Showing 20 of 31 experimental structures (best resolution first).
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