Nuclear receptor coactivator 1 (NCOA1) is a 1441-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15788.
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The mean pLDDT of this model is 46.7 (very 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 | 9% |
| 70 to 90 | Confident: backbone generally right | 11% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 72% |
What pLDDT means and how to read it
Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and…
Interacts with PPARA; the interaction is direct (PubMed:11698662). Interacts with PPARG; the interaction is direct (PubMed:11698662, PubMed:9744270). Interacts with ESRRG; the interaction is direct (PubMed:11864604). Interacts with STAT5A (via FDL motif) (PubMed:12954634). Interacts with STAT5B (via FDL motif) (PubMed:12954634). Interacts with STAT6 (via LXXLL motif) (PubMed:12138096). Interacts…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9GC7 | X-ray | 1.46 Å | B=1430-1441 |
| 1NQ7 | X-ray | 1.5 Å | B=687-696 |
| 3OLL | X-ray | 1.5 Å | C/D=683-701 |
| 7BQ1 | X-ray | 1.52 Å | B=683-697 |
| 7BQ2 | X-ray | 1.52 Å | B=683-697 |
| 6GEV | X-ray | 1.54 Å | B=1427-1441 |
| 7XVY | X-ray | 1.54 Å | C/D=628-640 |
| 3UUD | X-ray | 1.6 Å | C/D=686-698 |
| 6W9I | X-ray | 1.61 Å | A=683-696 |
| 7BQ4 | X-ray | 1.62 Å | B=683-697 |
| 7KXD | X-ray | 1.62 Å | A=683-696 |
| 8HUQ | X-ray | 1.65 Å | B=683-697 |
| 5HJS | X-ray | 1.72 Å | C/D=676-700 |
| 5MWY | X-ray | 1.75 Å | B=1427-1441 |
| 7BQ0 | X-ray | 1.77 Å | B/D=683-697 |
| 2P54 | X-ray | 1.79 Å | B=686-696 |
| 3KMR | X-ray | 1.8 Å | C=686-698 |
| 4MGA | X-ray | 1.8 Å | C/D=686-698 |
| 5Q0K | X-ray | 1.8 Å | B=744-757 |
| 5Q0P | X-ray | 1.8 Å | B/D=744-757 |
Showing 20 of 300 experimental structures (best resolution first).
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