Runt-related transcription factor 1 (Runx1) is a 451-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q03347.
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The mean pLDDT of this model is 61.1 (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 | 26% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 53% |
What pLDDT means and how to read it
Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis. Acts synergistically…
Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with TLE1 and ALYREF/THOC4. Interacts with HIPK2, ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may act to repress RUNX1-mediated transactivation. Interacts with KAT6A and KAT6B.…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1EAQ | X-ray | 1.25 Å | A/B=46-185 |
| 1EAO | X-ray | 1.4 Å | A/B=46-185 |
| 1EAN | X-ray | 1.7 Å | A=46-185 |
| 4L18 | X-ray | 2.3 Å | A/E=48-214 |
| 3WTS | X-ray | 2.35 Å | A/F=60-263 |
| 3WTT | X-ray | 2.35 Å | A/F=60-263 |
| 3WU1 | X-ray | 2.4 Å | A=55-177 |
| 4L0Y | X-ray | 2.5 Å | A=1-242 |
| 2J6W | X-ray | 2.6 Å | A/B=46-185 |
| 1HJC | X-ray | 2.65 Å | A/D=60-182 |
| 3WTU | X-ray | 2.7 Å | A/F=60-263 |
| 3WTV | X-ray | 2.7 Å | A/F=60-263 |
| 3WTY | X-ray | 2.7 Å | A/F=60-263 |
| 4L0Z | X-ray | 2.7 Å | A=1-242 |
| 3WTX | X-ray | 2.8 Å | A/F=60-263 |
| 3WTW | X-ray | 2.9 Å | A/F=60-263 |
| 1HJB | X-ray | 3.0 Å | C/F=60-182 |
| 1IO4 | X-ray | 3.0 Å | C=60-182 |
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