Eukaryotic translation initiation factor 2 subunit 1 (EIF2S1) is a 315-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05198.
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The mean pLDDT of this model is 77.8 (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 | 3% |
| 70 to 90 | Confident: backbone generally right | 81% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:16289705, PubMed:38340717). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (43S PIC) (PubMed:16289705). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex (PubMed:16289705). In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (PubMed:16289705). EIF2S1/eIF2-alpha is a…
Eukaryotic translation initiation factor 2 eIF2 is a heterotrimeric complex composed of an alpha (EIF2S1), a beta (EIF2S2) and a gamma (EIF2S3) chain (PubMed:23063529, PubMed:31048492, PubMed:31836389, PubMed:35031321). eIF2 is member of the 43S pre-initiation complex (43S PIC). eIF2 forms a complex with at least CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By similarity).…
Cytoplasm, Stress granule, Cytoplasm, cytosol, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1KL9 | X-ray | 1.9 Å | A=2-183 |
| 8PPL | EM | 2.65 Å | Ir=1-315 |
| 9HVE | EM | 2.7 Å | K/L=1-315 |
| 7F66 | EM | 2.76 Å | N=1-315 |
| 6ZP4 | EM | 2.9 Å | O=1-315 |
| 6O85 | EM | 3.03 Å | L=2-315 |
| 6O9Z | EM | 3.03 Å | L/M=2-315 |
| 9NB9 | EM | 3.03 Å | A=2-187 |
| 9HVD | EM | 3.04 Å | K/L=1-315 |
| 8PJ4 | EM | 3.2 Å | r=1-315 |
| 6O81 | EM | 3.21 Å | L/M=1-315 |
| 8QZZ | X-ray | 3.35 Å | B=1-315 |
| 8PJ1 | EM | 3.4 Å | r=1-315 |
| 8PJ2 | EM | 3.4 Å | r=1-315 |
| 7A09 | EM | 3.5 Å | O=1-315 |
| 7SYS | EM | 3.5 Å | j=1-315 |
| 8OZ0 | EM | 3.5 Å | D=1-315 |
| 7F67 | EM | 3.59 Å | N/Q=1-315 |
| 7SYR | EM | 3.6 Å | j=1-315 |
| 6ZMW | EM | 3.7 Å | r=1-315 |
Showing 20 of 32 experimental structures (best resolution first).
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