Neurogenic locus notch homolog protein 1 (NOTCH1) is a 2555-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P46531.
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The mean pLDDT of this model is 59.6 (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 | 3% |
| 70 to 90 | Confident: backbone generally right | 32% |
| 50 to 70 | Low: treat with caution | 39% |
| Below 50 | Very low: often disordered regions | 27% |
What pLDDT means and how to read it
Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the…
Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1 (PubMed:11101851, PubMed:12370315). The NOTCH1 intracellular domain interacts with SNW1; the interaction involves multimerized…
Cell membrane, Late endosome membrane, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5L0R | X-ray | 1.5 Å | B=452-491 |
| 9B3N | X-ray | 1.5 Å | A=753-944 |
| 2F8Y | X-ray | 1.55 Å | A/B=1905-2126 |
| 9B3G | X-ray | 1.55 Å | A=790-906 |
| 4D0E | X-ray | 1.61 Å | A=411-526 |
| 4CUD | X-ray | 1.85 Å | A=410-526 |
| 1YYH | X-ray | 1.9 Å | A/B=1872-2114 |
| 2HE0 | X-ray | 1.9 Å | A/B=1872-2116 |
| 3ETO | X-ray | 2.0 Å | A/B=1446-1733 |
| 5UB5 | X-ray | 2.09 Å | B=452-491 |
| 3L95 | X-ray | 2.19 Å | X/Y=1448-1728 |
| 4CUF | X-ray | 2.29 Å | A=411-526 |
| 5FMA | X-ray | 2.46 Å | A/B=142-294 |
| 2VJ3 | X-ray | 2.6 Å | A=410-529 |
| 6IDF | EM | 2.7 Å | E=1721-1847 |
| 4D0F | X-ray | 2.8 Å | A=411-526 |
| 5FM9 | X-ray | 2.92 Å | A=140-294 |
| 4CUE | X-ray | 3.0 Å | A=411-526 |
| 3I08 | X-ray | 3.2 Å | A/C=1446-1664, B/D=1665-1733 |
| 2F8X | X-ray | 3.25 Å | K=1872-2126 |
Showing 20 of 29 experimental structures (best resolution first).
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