Apolipoprotein E (APOE) is a 317-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02649.
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The mean pLDDT of this model is 75.5 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 42% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:14754908, PubMed:1911868, PubMed:6860692). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:14754908, PubMed:1911868, PubMed:1917954, PubMed:23620513, PubMed:2762297, PubMed:6860692, PubMed:9395455). Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:2762297, PubMed:6860692, PubMed:9395455). As such, APOE associates with…
Homotetramer (PubMed:8340399). May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs (PubMed:14754908). May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear (PubMed:23620513, PubMed:8367470). May interact with MAPT (PubMed:7972031). May interact with MAP2 (PubMed:7891887). In the…
Secreted, Secreted, extracellular space, Secreted, extracellular space, extracellular matrix, Extracellular vesicle, Endosome, multivesicular body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7FCR | X-ray | 1.4 Å | A=19-209 |
| 8AX8 | X-ray | 1.55 Å | A=19-317 |
| 8AX9 | X-ray | 1.55 Å | A=19-317 |
| 7FCS | X-ray | 1.6 Å | A=19-209 |
| 1GS9 | X-ray | 1.7 Å | A=19-183 |
| 6NCO | X-ray | 1.71 Å | A=19-180 |
| 1OR3 | X-ray | 1.73 Å | A=19-183 |
| 8CE0 | X-ray | 1.75 Å | A=19-317 |
| 1NFN | X-ray | 1.8 Å | A=19-209 |
| 6NCN | X-ray | 1.82 Å | A=19-180 |
| 1BZ4 | X-ray | 1.85 Å | A=40-183 |
| 1H7I | X-ray | 1.9 Å | A=19-209 |
| 8CDY | X-ray | 1.9 Å | A=19-317 |
| 1EA8 | X-ray | 1.95 Å | A=19-209 |
| 7UVJ | X-ray | 1.99 Å | A/B=40-183 |
| 1B68 | X-ray | 2.0 Å | A=19-209 |
| 1NFO | X-ray | 2.0 Å | A=19-209 |
| 6V7M | X-ray | 2.0 Å | A=1-100, B=101-183 |
| 1LPE | X-ray | 2.25 Å | A=41-184 |
| 1LE4 | X-ray | 2.5 Å | A=41-184 |
Showing 20 of 29 experimental structures (best resolution first).
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