Eukaryotic translation initiation factor 4E (EIF4E) is a 217-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06730.
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The mean pLDDT of this model is 90.9 (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 | 82% |
| 70 to 90 | Confident: backbone generally right | 5% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 5% |
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:11606200, PubMed:22578813, PubMed:22684010, PubMed:24335285, PubMed:29987188). 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 (By similarity). 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 (PubMed:11408474, PubMed:11879179, PubMed:16271312, PubMed:17631896). It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3 (PubMed:11408474, PubMed:11879179, PubMed:12975586, PubMed:29987188, PubMed:8521827). EIF4E is also known to interact with other partners…
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 |
|---|---|---|---|
| 4TPW | X-ray | 1.5 Å | A/B=28-217 |
| 5T46 | X-ray | 1.53 Å | A/C=1-217 |
| 8QM8 | X-ray | 1.58 Å | A/B=36-217 |
| 4TQB | X-ray | 1.59 Å | A/B=28-217 |
| 5ZJY | X-ray | 1.59 Å | A=28-217 |
| 5ZJZ | X-ray | 1.67 Å | A=28-217 |
| 7D6Y | X-ray | 1.67 Å | A=1-217 |
| 5EI3 | X-ray | 1.71 Å | A=1-217 |
| 4UED | X-ray | 1.75 Å | A=36-217 |
| 5ZK9 | X-ray | 1.76 Å | A=28-217 |
| 4TQC | X-ray | 1.8 Å | A/B=28-217 |
| 5ZML | X-ray | 1.8 Å | A=27-217 |
| 7XTP | X-ray | 1.83 Å | A/B=1-217 |
| 8QM4 | X-ray | 1.85 Å | A/B=36-217 |
| 8QM5 | X-ray | 1.89 Å | A/B=36-217 |
| 7MEU | X-ray | 1.91 Å | A/B=26-217 |
| 8QM6 | X-ray | 1.93 Å | A/B=36-217 |
| 5GW6 | X-ray | 1.97 Å | A=23-217 |
| 8QM9 | X-ray | 1.97 Å | A/B=36-217 |
| 8SX4 | X-ray | 1.99 Å | A/B=28-217 |
Showing 20 of 45 experimental structures (best resolution first).
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