Estrogen receptor (ESR1) is a 595-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P03372.
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The mean pLDDT of this model is 66.4 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 46% |
What pLDDT means and how to read it
Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression…
Binds DNA as a homodimer. Can form a heterodimer with ESR2. Interacts with FOXC2, MAP1S, SLC30A9, UBE1C and NCOA3 coactivator (By similarity). Interacts with PELP1, the interaction is enhanced by 17-beta-estradiol, the interaction increases ESR1 transcriptional activity (PubMed:11481323, PubMed:14963108). Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1.…
Nucleus, Cytoplasm, Cell membrane, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7BAA | X-ray | 1.1 Å | B=588-595 |
| 8BZC | X-ray | 1.1 Å | B=591-595 |
| 8BZW | X-ray | 1.1 Å | B=590-595 |
| 8C04 | X-ray | 1.1 Å | B=591-595 |
| 7B9R | X-ray | 1.15 Å | B=588-595 |
| 7B9T | X-ray | 1.15 Å | B=588-595 |
| 7NFW | X-ray | 1.19 Å | B=588-595 |
| 6HMU | X-ray | 1.2 Å | B=588-595 |
| 7BA8 | X-ray | 1.2 Å | B=588-595 |
| 8APS | X-ray | 1.2 Å | B=591-595 |
| 8BX3 | X-ray | 1.2 Å | B=591-595 |
| 8BXI | X-ray | 1.2 Å | B=591-595 |
| 8BYO | X-ray | 1.2 Å | B=591-595 |
| 8BZ0 | X-ray | 1.2 Å | B=591-595 |
| 8BZA | X-ray | 1.25 Å | B=591-595 |
| 7BAB | X-ray | 1.3 Å | B=588-595 |
| 8BZ9 | X-ray | 1.3 Å | B=591-595 |
| 9I6S | X-ray | 1.3 Å | B=591-595 |
| 9I6T | X-ray | 1.3 Å | B=591-595 |
| 9I6U | X-ray | 1.3 Å | B=591-595 |
Showing 20 of 478 experimental structures (best resolution first).
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