HLA class I histocompatibility antigen, alpha chain E (HLA-E) is a 358-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13747.
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The mean pLDDT of this model is 87.0 (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 | 75% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Non-classical major histocompatibility class Ib molecule involved in immune self-nonself discrimination. In complex with B2M/beta-2-microglobulin binds nonamer self-peptides derived from the signal sequence of classical MHC class Ia molecules (VL9 peptides - VMAPRT[V/L][L/V/I/F]L) (PubMed:18083576, PubMed:18339401, PubMed:35705051, PubMed:37264229, PubMed:9754572). Peptide-bound HLA-E-B2M heterotrimeric complex primarily functions as a ligand for natural killer (NK) cell inhibitory receptor KLRD1-KLRC1, enabling NK cells to monitor the expression of other MHC class I molecules in healthy cells and to tolerate self (PubMed:17179229, PubMed:18083576, PubMed:37264229, PubMed:9486650,…
Forms a heterotrimer with B2M and a self- or a pathogen-derived peptide (peptide-bound HLA-E-B2M) (PubMed:18339401, PubMed:30087334, PubMed:35705051). Similarly to MHC class Ia assembly, HLA-E-B2M heterodimer interacts with components of the antigen processing machinery TAPBP and TAP1-TAP2 complex; this interaction is required for peptide loading and translocation to the cell surface…
Cell membrane, Golgi apparatus membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7P4B | X-ray | 1.72 Å | A/C/E/G=22-297 |
| 7BH8 | X-ray | 1.8 Å | A/C=22-297 |
| 7P49 | X-ray | 2.05 Å | A/C/E/G=22-297 |
| 6GH1 | X-ray | 2.1 Å | A/C/E/G=22-295 |
| 9NW7 | X-ray | 2.1 Å | A=22-295 |
| 6GH4 | X-ray | 2.16 Å | A/C/E/G=22-295 |
| 6ZKX | X-ray | 2.17 Å | A=22-297 |
| 8RLT | X-ray | 2.25 Å | A/F=22-297 |
| 6ZKW | X-ray | 2.26 Å | A=22-297 |
| 6ZKZ | X-ray | 2.3 Å | A=22-297 |
| 9NW8 | X-ray | 2.3 Å | A=22-295 |
| 9NW9 | X-ray | 2.3 Å | A=22-295 |
| 8QFY | X-ray | 2.33 Å | AAA/FFF=22-297 |
| 8RLU | X-ray | 2.35 Å | A/F=22-297 |
| 3BZE | X-ray | 2.5 Å | A/C/E/G=23-295 |
| 3BZF | X-ray | 2.5 Å | A/C=22-297 |
| 6GHN | X-ray | 2.54 Å | A/C=22-295 |
| 7NDQ | X-ray | 2.55 Å | AAA=22-297 |
| 2ESV | X-ray | 2.6 Å | A=23-297 |
| 8RLV | X-ray | 2.61 Å | A/F=22-297 |
Showing 20 of 34 experimental structures (best resolution first).
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