Eukaryotic peptide chain release factor subunit 1 (ETF1) is a 437-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62495.
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The mean pLDDT of this model is 85.1 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 46% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:10676813, PubMed:16777602, PubMed:24486019, PubMed:26245381, PubMed:27863242, PubMed:36638793, PubMed:7990965). The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:26245381, PubMed:27863242, PubMed:36638793). ETF1/ERF1 is responsible for stop codon recognition and inducing hydrolysis of peptidyl-tRNA (PubMed:26245381, PubMed:27863242, PubMed:36638793). Following GTP hydrolysis, eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) dissociates, permitting ETF1/eRF1 to accommodate fully in the A-site and mediate hydrolysis of…
Component of the eRF1-eRF3-GTP ternary complex, composed of ETF1/ERF1 and eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) and GTP (PubMed:19417105, PubMed:27863242). Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). Interacts with JMJD4 (PubMed:24486019). The ETF1-GSPT1 complex interacts with JMJD4 (PubMed:24486019)
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9I2D | EM | 2.19 Å | CR=1-437 |
| 8ZHC | EM | 2.3 Å | eR=1-437 |
| 9S3D | EM | 2.32 Å | CR=1-437 |
| 9S3B | EM | 2.38 Å | CR=1-437 |
| 9S3C | EM | 2.42 Å | CR=1-437 |
| 9QLO | EM | 2.47 Å | CR=1-437 |
| 8SCB | EM | 2.5 Å | ii=1-437 |
| 9QLQ | EM | 2.57 Å | CR=1-437 |
| 9RHU | EM | 2.65 Å | p2=2-437 |
| 1DT9 | X-ray | 2.7 Å | A=1-437 |
| 9QLP | EM | 2.75 Å | CR=1-437 |
| 6XA1 | EM | 2.8 Å | j=11-421 |
| 6ZME | EM | 3.0 Å | CH=1-437 |
| 6D90 | EM | 3.2 Å | jj=1-437 |
| 5LZV | EM | 3.35 Å | ii=1-437 |
| 3JAH | EM | 3.45 Å | ii=6-421 |
| 3JAG | EM | 3.65 Å | ii=6-421 |
| 3JAI | EM | 3.65 Å | ii=6-421 |
| 5LZT | EM | 3.65 Å | ii=1-437 |
| 5LZU | EM | 3.75 Å | ii=1-437 |
Showing 20 of 33 experimental structures (best resolution first).
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