Myc proto-oncogene protein (MYC) is a 454-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01106.
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The mean pLDDT of this model is 60.4 (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 | 19% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 36% |
| Below 50 | Very low: often disordered regions | 41% |
What pLDDT means and how to read it
Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of…
Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (PubMed:9680483). Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-73 and Ser-77) with FBXW7 (PubMed:17558397, PubMed:25775507). Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with…
Nucleus, nucleoplasm, Nucleus, nucleolus, Nucleus, Cytoplasm, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9QNH | X-ray | 1.3 Å | P=290-298 |
| 6G6K | X-ray | 1.35 Å | A/C=366-452 |
| 1NKP | X-ray | 1.8 Å | A/D=368-449 |
| 8Q1N | X-ray | 1.84 Å | a/b=273-283 |
| 4Y7R | X-ray | 1.9 Å | B=275-282 |
| 8J2Q | X-ray | 1.92 Å | A=417-427 |
| 5I4Z | X-ray | 1.95 Å | A/B=363-454 |
| 8X8V | X-ray | 2.0 Å | A=417-427 |
| 8X8S | X-ray | 2.04 Å | A=417-427 |
| 1EE4 | X-ray | 2.1 Å | C/D/E/F=335-343 |
| 6G6L | X-ray | 2.2 Å | A/C/E/G=366-452 |
| 6G6J | X-ray | 2.25 Å | A/C=366-452 |
| 6E16 | X-ray | 2.4 Å | A=111-140 |
| 7T1Y | X-ray | 2.55 Å | C=250-280 |
| 8WLG | X-ray | 2.55 Å | A=417-426 |
| 6C4U | X-ray | 2.6 Å | G/H/I/J/K/L=69-77 |
| 2OR9 | X-ray | 2.7 Å | P=425-434 |
| 5I50 | X-ray | 2.7 Å | A/B=365-454 |
| 7T1Z | X-ray | 2.77 Å | C=62-81 |
| 6E24 | X-ray | 3.0 Å | A=111-140 |
Showing 20 of 25 experimental structures (best resolution first).
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