Replication factor C subunit 3 (RFC3) is a 340-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P38629.
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The mean pLDDT of this model is 90.8 (very high 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 | 80% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. 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. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA…
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. Component of the RAD24-RFC complex which consists of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8DQW | EM | 2.1 Å | C=1-340 |
| 8DQX | EM | 2.1 Å | C=1-340 |
| 8DR1 | EM | 2.14 Å | C=1-340 |
| 7ST9 | EM | 2.2 Å | C=1-340 |
| 8DR3 | EM | 2.2 Å | C=1-340 |
| 8DR6 | EM | 2.39 Å | C=1-340 |
| 8DR0 | EM | 2.42 Å | C=1-340 |
| 8DR4 | EM | 2.45 Å | C=1-340 |
| 9PEO | EM | 2.57 Å | C=1-340 |
| 9PER | EM | 2.57 Å | C=1-340 |
| 9PET | EM | 2.57 Å | C=1-340 |
| 9PES | EM | 2.59 Å | C=1-340 |
| 9PEU | EM | 2.62 Å | C=1-340 |
| 9PEV | EM | 2.63 Å | C=1-340 |
| 8DR7 | EM | 2.7 Å | C=1-340 |
| 7STB | EM | 2.72 Å | C=1-340 |
| 7STE | EM | 2.73 Å | C=1-339 |
| 8DR5 | EM | 2.76 Å | C=1-340 |
| 8FS5 | EM | 2.76 Å | C=1-336 |
| 1SXJ | X-ray | 2.85 Å | C=1-340 |
Showing 20 of 50 experimental structures (best resolution first).
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