Eukaryotic translation initiation factor 3 subunit M (EIF3M) is a 374-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7L2H7.
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The mean pLDDT of this model is 55.3 (low 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 | 0% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 71% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17403899, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to…
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C,…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8PPL | EM | 2.65 Å | I6=1-374 |
| 6ZP4 | EM | 2.9 Å | M=1-374 |
| 8PJ5 | EM | 2.9 Å | 6=1-374 |
| 8PJ6 | EM | 2.9 Å | 6=1-374 |
| 6ZON | EM | 3.0 Å | M=1-374 |
| 9KZU | EM | 3.0 Å | 3m=1-374 |
| 8PJ4 | EM | 3.2 Å | 6=1-374 |
| 9KN5 | EM | 3.2 Å | 3m=1-374 |
| 9KRP | EM | 3.2 Å | 3m=1-374 |
| 6YBD | EM | 3.3 Å | 6=1-374 |
| 9KKF | EM | 3.3 Å | 3m=1-374 |
| 9KN6 | EM | 3.3 Å | 3m=1-374 |
| 9KZX | EM | 3.3 Å | 3m=1-374 |
| 8PJ1 | EM | 3.4 Å | 6=1-374 |
| 8PJ2 | EM | 3.4 Å | 6=1-374 |
| 8RG0 | EM | 3.4 Å | 6=1-374 |
| 7A09 | EM | 3.5 Å | M=1-374 |
| 8OZ0 | EM | 3.5 Å | C=1-374 |
| 8XXN | EM | 3.6 Å | 3M=1-374 |
| 6ZMW | EM | 3.7 Å | 6=1-374 |
Showing 20 of 28 experimental structures (best resolution first).
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