Eukaryotic translation initiation factor 5A-1 (HYP2) is a 157-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P23301.
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The mean pLDDT of this model is 88.1 (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 | 78% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:10229683, PubMed:16157662, PubMed:16914118, PubMed:19338753, PubMed:19424157, PubMed:23727016, PubMed:24923804, PubMed:28392174, PubMed:36804914, PubMed:641056, PubMed:8307948, PubMed:9582285). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (PubMed:23727016, PubMed:24923804, PubMed:28392174). Acts as a ribosome quality control (RQC) cofactor by…
Homodimer (PubMed:19120453). Binds to 80S ribosomes (PubMed:16215987, PubMed:27115996). Actively translating ribosomes show mutually exclusive binding of eIF5a (HYP2 or ANB1) and EFT1/eEF2 (PubMed:27115996). Interacts with DYS1 and LIA1 (PubMed:14675757, PubMed:16215987)
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8AGX | EM | 2.4 Å | v=1-157 |
| 8BN3 | EM | 2.4 Å | eI=10-154 |
| 8AAF | EM | 2.5 Å | v=1-157 |
| 8AGT | EM | 2.6 Å | v=1-157 |
| 8AGV | EM | 2.6 Å | v=1-157 |
| 8AGZ | EM | 2.6 Å | v=1-157 |
| 8AGU | EM | 2.7 Å | v=1-157 |
| 6TNU | EM | 3.1 Å | eI=4-157 |
| 5DAT | X-ray | 3.15 Å | f=1-157 |
| 8K2D | EM | 3.2 Å | CE=1-157 |
| 8UT0 | EM | 3.22 Å | Ls=1-157 |
| 5DC3 | X-ray | 3.25 Å | f=1-157 |
| 5DGF | X-ray | 3.3 Å | f=1-157 |
| 3ER0 | X-ray | 3.35 Å | A/B=1-157 |
| 5DGE | X-ray | 3.45 Å | f=1-157 |
| 8Y0U | EM | 3.59 Å | 5=1-157 |
| 6Q84 | X-ray | 3.7 Å | C/F=16-157 |
| 5MC6 | EM | 3.8 Å | BT=1-157 |
| 5GAK | EM | 3.88 Å | q=1-157 |
| 7NRC | EM | 3.9 Å | Ls=4-157 |
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