Nuclear receptor corepressor 2 (NCOR2) is a 2514-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y618.
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The mean pLDDT of this model is 40.2 (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 | 2% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 84% |
What pLDDT means and how to read it
Transcriptional corepressor that mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription (PubMed:10077563, PubMed:10097068, PubMed:18212045, PubMed:20812024, PubMed:22230954, PubMed:23911289). Acts by recruiting chromatin modifiers, such as histone deacetylases HDAC1, HDAC2 and HDAC3 (PubMed:22230954). Required to activate the histone deacetylase activity of HDAC3 (PubMed:22230954). Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival (PubMed:18212045, PubMed:23911289). Recruited by…
Forms a large corepressor complex that contains SIN3A/B and histone deacetylases HDAC1 and HDAC2. This complex associates with the thyroid (TR) and the retinoid acid receptors (RAR) in the absence of ligand, and may stabilize their interaction with TFIIB. Interacts directly with RARA in the absence of ligand; the interaction represses RARA activity. Interacts (isoform SMRT) with HDAC10.…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8B94 | X-ray | 1.55 Å | C/D=2332-2354 |
| 8B92 | X-ray | 1.66 Å | C/D=2332-2354 |
| 8B95 | X-ray | 1.72 Å | C/D=2332-2354 |
| 8B8X | X-ray | 1.78 Å | C/D=2332-2354 |
| 5ZOO | X-ray | 1.85 Å | A=1350-1363 |
| 8B8W | X-ray | 1.86 Å | C/D=2332-2354 |
| 8AQN | X-ray | 1.9 Å | C/D=2332-2354 |
| 8B8Y | X-ray | 2.0 Å | C/D=2332-2354 |
| 4A69 | X-ray | 2.06 Å | C/D=389-480 |
| 6PDZ | X-ray | 2.1 Å | C/D=2335-2356 |
| 8B90 | X-ray | 2.1 Å | C/D=2332-2354 |
| 9XMJ | X-ray | 2.18 Å | B/D/F/H=2335-2356 |
| 1R2B | X-ray | 2.2 Å | C/D=1414-1430 |
| 5X8Q | X-ray | 2.2 Å | B/D/F/H=2335-2356 |
| 8B93 | X-ray | 2.21 Å | C/D=2332-2354 |
| 8B8Z | X-ray | 2.22 Å | C/D=2332-2354 |
| 8B91 | X-ray | 2.23 Å | C/D=2332-2354 |
| 8AQM | X-ray | 2.3 Å | C/D=2332-2354 |
| 8X7E | X-ray | 2.3 Å | B/D/F/H=2335-2356 |
| 6IVX | X-ray | 2.35 Å | B/D/F/H=2335-2356 |
Showing 20 of 36 experimental structures (best resolution first).
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