TNF receptor-associated factor 6 (TRAF6) is a 522-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y4K3.
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The mean pLDDT of this model is 84.2 (confident 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 | 71% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2 (PubMed:11057907, PubMed:18347055, PubMed:19465916, PubMed:19713527, PubMed:27746020, PubMed:31620128). Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation (PubMed:19675569). Leads to the activation of NF-kappa-B and JUN (PubMed:16378096, PubMed:17135271, PubMed:17703191, PubMed:39920527, PubMed:40973797, PubMed:41747053). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated…
Homotrimer. Homooligomer. N-terminal region is dimeric while C-terminal region is trimeric; maybe providing a mode of oligomerization. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR…
Cytoplasm, Cytoplasm, cell cortex, Nucleus, Lipid droplet
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1LB6 | X-ray | 1.8 Å | A=347-504 |
| 3HCT | X-ray | 2.1 Å | A=50-159 |
| 6A33 | X-ray | 2.1 Å | A=350-501 |
| 3HCS | X-ray | 2.2 Å | A/B=50-211 |
| 1LB4 | X-ray | 2.4 Å | A=348-504 |
| 1LB5 | X-ray | 2.4 Å | A=347-504 |
| 3HCU | X-ray | 2.6 Å | A/C=50-159 |
| 5ZUJ | X-ray | 2.6 Å | A=350-501 |
| 8HZ2 | X-ray | 2.6 Å | A/B=54-210 |
| 7L3L | X-ray | 2.8 Å | B/D=52-158 |
| 4Z8M | X-ray | 2.95 Å | A/B=346-504 |
| 2ECI | NMR | A=50-128 | |
| 2JMD | NMR | A=67-124 |
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