Elongation factor 2 (EEF2) is a 858-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13639.
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The mean pLDDT of this model is 89.8 (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 | 65% |
| 70 to 90 | Confident: backbone generally right | 32% |
| 50 to 70 | Low: treat with caution | 4% |
| 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:26593721). 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:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721)
Binds to 80S ribosomes (PubMed:27115996, PubMed:30355441). Actively translating ribosomes show mutually exclusive binding of eIF5a (EIF5A or EIF5A2) and EEF2/eEF2 (PubMed:27115996). Interacts with SERBP1; interaction sequesters EEF2/eEF2 at the A-site of the ribosome, thereby blocking the interaction sites of the mRNA-tRNA complex, promoting ribosome stabilization and hibernation…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8XSX | EM | 2.4 Å | CB=1-858 |
| 9P7D | EM | 2.57 Å | CB=3-858 |
| 9P7E | EM | 2.59 Å | CB=3-858 |
| 9P73 | EM | 2.66 Å | CB=3-858 |
| 9P9I | EM | 2.77 Å | CB=3-858 |
| 9M0P | EM | 2.78 Å | CA=1-858 |
| 9P7C | EM | 2.78 Å | CB=3-858 |
| 9P7A | EM | 2.81 Å | CB=3-858 |
| 9B0P | EM | 2.82 Å | CB=3-858 |
| 9P9H | EM | 2.84 Å | CB=3-858 |
| 9FQZ | EM | 2.85 Å | CB=1-858 |
| 6Z6N | EM | 2.9 Å | CB=1-858 |
| 9P78 | EM | 2.9 Å | CB=3-858 |
| 9I2E | EM | 2.95 Å | CB=1-858 |
| 8UKB | EM | 3.05 Å | CB=3-858 |
| 6Z6M | EM | 3.1 Å | CB=1-858 |
| 9P79 | EM | 3.1 Å | CB=3-858 |
| 9P8C | EM | 3.11 Å | CB=3-858 |
| 6D9J | EM | 3.2 Å | 9=3-858 |
| 9B0Q | EM | 3.2 Å | CB/cB=3-858 |
Showing 20 of 24 experimental structures (best resolution first).
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