Translation initiation factor eIF2B subunit alpha (EIF2B1) is a 305-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14232.
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The mean pLDDT of this model is 91.8 (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 | 72% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on eukaryotic initiation factor 2 (eIF2) gamma subunit (PubMed:25858979, PubMed:27023709, PubMed:31048492). Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed (PubMed:25858979, PubMed:31048492)
Component of the translation initiation factor 2B (eIF2B) complex which is a heterodecamer of two sets of five different subunits: alpha, beta, gamma, delta and epsilon. Subunits alpha, beta and delta comprise a regulatory subcomplex and subunits epsilon and gamma comprise a catalytic subcomplex (PubMed:25858979, PubMed:27023709, PubMed:31048492). Within the complex, the hexameric regulatory…
Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9ZUZ | X-ray | 2.25 Å | A=1-305 |
| 7VLK | EM | 2.27 Å | A/B=1-305 |
| 7F64 | EM | 2.42 Å | A/B=1-305 |
| 7RLO | EM | 2.6 Å | G/H=1-305 |
| 3ECS | X-ray | 2.65 Å | A/B/C/D/E/F/G/H=1-305 |
| 7KMA | X-ray | 2.7 Å | A/B/C/D/E/F/G/H=1-305 |
| 9HVE | EM | 2.7 Å | A/B=1-305 |
| 7F66 | EM | 2.76 Å | A/B=1-305 |
| 6CAJ | EM | 2.8 Å | G/H=1-305 |
| 7L70 | EM | 2.8 Å | G/H=2-305 |
| 7TRJ | EM | 2.8 Å | G/H=1-305 |
| 8TQZ | EM | 2.9 Å | G/H=2-305 |
| 7KMF | EM | 2.91 Å | G/H=1-305 |
| 7L7G | EM | 3.0 Å | G/H=1-305 |
| 6O85 | EM | 3.03 Å | G/H=1-305 |
| 6O9Z | EM | 3.03 Å | G/H=1-305 |
| 9HVD | EM | 3.04 Å | A/B=1-305 |
| 6O81 | EM | 3.21 Å | G/H=1-305 |
| 7F67 | EM | 3.59 Å | A/B=1-305 |
| 7D45 | EM | 3.8 Å | A/B=1-305 |
Showing 20 of 26 experimental structures (best resolution first).
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