Eukaryotic translation initiation factor 4E (Eif4e) is a 217-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63073.
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The mean pLDDT of this model is 90.5 (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 | 81% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed:18805096, PubMed:25456498, PubMed:31042468, PubMed:36843541, PubMed:8577715). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:18805096). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome…
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions (By similarity). It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3 (PubMed:9200613). EIF4E is also known to interact with other partners (By similarity). Interacts with EIF4ENIF1/4E-T; promotes recruitment to P-bodies and import into the nucleus (By similarity).…
Cytoplasm, P-body, Cytoplasm, Cytoplasm, Stress granule, Nucleus, Nucleus speckle, Nucleus, nuclear body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5M7X | X-ray | 1.68 Å | A/B/C/D=28-217 |
| 5M7Z | X-ray | 1.69 Å | A/B/C/D=28-217 |
| 5M7V | X-ray | 1.74 Å | A/B/C/D=28-217 |
| 5J5Y | X-ray | 1.75 Å | A/B/C/D=28-217 |
| 6U09 | X-ray | 1.79 Å | A/B/C/D=28-217 |
| 1L8B | X-ray | 1.8 Å | A/B=28-217 |
| 5M84 | X-ray | 1.85 Å | A/B=28-217 |
| 5M83 | X-ray | 1.86 Å | A/B=28-217 |
| 6GKK | X-ray | 1.86 Å | A/B/C/D=28-217 |
| 5J5O | X-ray | 1.87 Å | A/B/C/D=28-217 |
| 5M81 | X-ray | 1.9 Å | A/B/C/D=28-217 |
| 5OSX | X-ray | 1.92 Å | A/B/C/D=28-217 |
| 6U06 | X-ray | 1.96 Å | A/B/C/D=28-217 |
| 5M7W | X-ray | 1.97 Å | A/B/C/D=28-217 |
| 6GKJ | X-ray | 2.07 Å | A/B/C/D=28-217 |
| 5BXV | X-ray | 2.1 Å | A/C=27-217 |
| 5M80 | X-ray | 2.12 Å | A/B/C/D=28-217 |
| 1EJ1 | X-ray | 2.2 Å | A/B=28-217 |
| 1EJH | X-ray | 2.2 Å | A/B/C/D=28-217 |
| 6GKL | X-ray | 2.2 Å | A/B/C/D=28-217 |
Showing 20 of 24 experimental structures (best resolution first).
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