Eukaryotic translation initiation factor 2 subunit 3 (EIF2S3) is a 472-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P41091.
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The mean pLDDT of this model is 85.1 (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 | 38% |
| 70 to 90 | Confident: backbone generally right | 56% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 2% |
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:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC) (By similarity). 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 (By similarity). 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 eIF-2B (By similarity)
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) (PubMed:23063529). Interacts (via C-terminus) with CDC123; the interaction is direct (PubMed:35031321, PubMed:37507029)
Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8PHV | X-ray | 1.97 Å | B/D=363-472 |
| 8PHD | X-ray | 2.08 Å | B/D=363-472 |
| 8PPL | EM | 2.65 Å | It=1-472 |
| 9HVE | EM | 2.7 Å | O/P=1-472 |
| 7F66 | EM | 2.76 Å | S=1-472 |
| 6ZP4 | EM | 2.9 Å | Y=1-472 |
| 6O85 | EM | 3.03 Å | S=1-472 |
| 8PJ4 | EM | 3.2 Å | t=1-472 |
| 6O81 | EM | 3.21 Å | S/T=1-472 |
| 8QZZ | X-ray | 3.35 Å | A=1-472 |
| 8PJ1 | EM | 3.4 Å | t=1-472 |
| 8PJ2 | EM | 3.4 Å | t=1-472 |
| 7A09 | EM | 3.5 Å | Y=1-472 |
| 8OZ0 | EM | 3.5 Å | E=1-472 |
| 7F67 | EM | 3.59 Å | S/T=1-472 |
| 6ZMW | EM | 3.7 Å | t=1-472 |
| 7QP7 | EM | 3.7 Å | t=1-472 |
| 8PJ3 | EM | 3.7 Å | t=1-472 |
| 6YBV | EM | 3.8 Å | t=1-472 |
| 9HVF | EM | 3.8 Å | D=1-472 |
Showing 20 of 25 experimental structures (best resolution first).
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