Elongation factor 2 (EFT1) is a 842-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P32324.
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The mean pLDDT of this model is 90.7 (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 | 70% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:14976550, PubMed:16950777, PubMed:17082187, PubMed:29069440). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:14976550, PubMed:16950777, PubMed:17082187). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:14976550, PubMed:16950777, PubMed:17082187)
Binds to 80S ribosomes (PubMed:12692531, PubMed:14976550, PubMed:15316019, PubMed:27115996). Actively translating ribosomes show mutually exclusive binding of eIF5a (HYP2 or ANB1) and EFT1/eEF2 (PubMed:27115996). Interacts with the 40S ribosomal subunit protein RPL9A; the interaction is direct (PubMed:14976550). Interacts with the 60S ribosomal subunit proteins RPL12A; the interaction is direct…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8CDR | EM | 2.04 Å | Aa=1-842 |
| 1N0U | X-ray | 2.12 Å | A=1-842 |
| 3B82 | X-ray | 2.35 Å | A/C/E=1-842 |
| 3B78 | X-ray | 2.5 Å | A/C/E=1-842 |
| 3B8H | X-ray | 2.5 Å | A/C/E=1-842 |
| 8EUB | EM | 2.52 Å | DC=1-842 |
| 1U2R | X-ray | 2.6 Å | A=1-842 |
| 8EVS | EM | 2.62 Å | DC=1-842 |
| 8EVQ | EM | 2.72 Å | DC=1-842 |
| 1ZM9 | X-ray | 2.8 Å | A/C/E=1-842 |
| 1N0V | X-ray | 2.85 Å | C/D=1-842 |
| 8T3A | EM | 2.86 Å | DC=1-842 |
| 8EVR | EM | 2.87 Å | DC=1-842 |
| 8EWB | EM | 2.87 Å | DC=1-842 |
| 1ZM4 | X-ray | 2.9 Å | A/C/E=1-842 |
| 2NPF | X-ray | 2.9 Å | A/B=1-842 |
| 8T3D | EM | 2.95 Å | DC=1-842 |
| 2ZIT | X-ray | 3.0 Å | A/C/E=1-842 |
| 8T3E | EM | 3.04 Å | DC=1-842 |
| 1ZM2 | X-ray | 3.07 Å | A/C/E=1-842 |
Showing 20 of 43 experimental structures (best resolution first).
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