Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1) is a 118-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13541.
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The mean pLDDT of this model is 71.4 (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 | 13% |
| 70 to 90 | Confident: backbone generally right | 44% |
| 50 to 70 | Low: treat with caution | 25% |
| Below 50 | Very low: often disordered regions | 18% |
What pLDDT means and how to read it
Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways
Hypophosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) or mTORC1 phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation (PubMed:12150926, PubMed:16271312, PubMed:17368478, PubMed:17631896, PubMed:22578813, PubMed:25702871, PubMed:7935836,…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2JGB | X-ray | 1.7 Å | B=51-67 |
| 4UED | X-ray | 1.75 Å | B=50-83 |
| 3HXI | X-ray | 1.8 Å | C=51-67 |
| 5NVN | X-ray | 1.9 Å | B/D=50-83 |
| 3M94 | X-ray | 2.05 Å | C=51-67 |
| 1WKW | X-ray | 2.1 Å | B=47-66 |
| 2V8Y | X-ray | 2.1 Å | B/F=51-64 |
| 3HXG | X-ray | 2.1 Å | C=51-67 |
| 3U7X | X-ray | 2.1 Å | C/D=47-66 |
| 5BXV | X-ray | 2.1 Å | B/D=43-84 |
| 1EJH | X-ray | 2.2 Å | E/F/G/H=54-66 |
| 1EJ4 | X-ray | 2.25 Å | B=51-64 |
| 2V8W | X-ray | 2.3 Å | B/F=51-64 |
| 2V8X | X-ray | 2.3 Å | B/F=51-64 |
| 2JGC | X-ray | 2.4 Å | B=51-67 |
| 3M93 | X-ray | 2.9 Å | C=51-67 |
| 5WBJ | X-ray | 3.0 Å | T=99-118 |
| 6BCX | EM | 3.0 Å | X/Z=1-118 |
| 8RCN | EM | 3.1 Å | X=1-118 |
| 9ED4 | EM | 3.23 Å | K/T=1-118 |
Showing 20 of 24 experimental structures (best resolution first).
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