Eukaryotic translation initiation factor 1A, X-chromosomal (EIF1AX) is a 144-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P47813.
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The mean pLDDT of this model is 77.9 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 26% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:9732867). This protein enhances formation of the cap-proximal complex (PubMed:9732867). Together with EIF1, facilitates scanning, start codon recognition, promotion of the assembly of 48S complex at the initiation codon (43S PIC becomes 48S PIC after the start codon is reached), and dissociation of aberrant complexes (PubMed:9732867). After start codon location, together with EIF5B orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex…
Component of the 43S pre-initiation complex (43S PIC), which is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3 complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary complex). Interacts with EIF5; this interaction contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994). Interacts through its C-terminal domain (CTD) with the CTD of EIF5B; from…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8PPL | EM | 2.65 Å | Iq=1-144 |
| 6ZP4 | EM | 2.9 Å | G=1-144 |
| 8PJ5 | EM | 2.9 Å | q=1-144 |
| 8PJ6 | EM | 2.9 Å | q=1-144 |
| 9H74 | EM | 2.9 Å | j=1-144 |
| 6YBW | EM | 3.1 Å | q=1-144 |
| 8PJ4 | EM | 3.2 Å | q=1-144 |
| 9KN5 | EM | 3.2 Å | 1A=1-144 |
| 9KN6 | EM | 3.3 Å | 1A=1-144 |
| 7TQL | EM | 3.4 Å | 4=24-113 |
| 8PJ1 | EM | 3.4 Å | q=1-144 |
| 8PJ2 | EM | 3.4 Å | q=1-144 |
| 7A09 | EM | 3.5 Å | G=1-112 |
| 7SYS | EM | 3.5 Å | A=1-144 |
| 8OZ0 | EM | 3.5 Å | G=1-144 |
| 3ZJY | X-ray | 3.6 Å | C=1-112 |
| 7SYR | EM | 3.6 Å | A=1-144 |
| 6ZMW | EM | 3.7 Å | q=1-144 |
| 7QP7 | EM | 3.7 Å | q=1-144 |
| 7SYW | EM | 3.7 Å | A=1-144 |
Showing 20 of 28 experimental structures (best resolution first).
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