TNF receptor-associated factor 2 (TRAF2) is a 501-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12933.
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The mean pLDDT of this model is 90.2 (very high 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 | 74% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis (PubMed:10346818, PubMed:11784851, PubMed:12917689, PubMed:15383523, PubMed:18981220, PubMed:19150425, PubMed:19810754, PubMed:19918265, PubMed:19937093, PubMed:20047764, PubMed:20064526, PubMed:20385093, PubMed:20577214, PubMed:22212761). Catalyzes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, IKBKE, MLST8, RIPK1 and TICAM1 (PubMed:23453969, PubMed:28489822). Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact…
Homotrimer (PubMed:8069916). Heterotrimer with TRAF1 (PubMed:8069916). Heterotrimer with TRAF3 (via TRAF domain) (PubMed:15383523, PubMed:20447407). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro) (PubMed:19810754). Interacts with TNFRSF1B/TNFR2 (PubMed:10206649, PubMed:7639698, PubMed:8069916). Interacts with TNFRSF5/CD40…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3KNV | X-ray | 1.9 Å | A=1-133 |
| 8T5Q | X-ray | 1.9 Å | A/B/C/D/E/F=315-501 |
| 1CZY | X-ray | 2.0 Å | A/B/C=334-501 |
| 1D00 | X-ray | 2.0 Å | A/B/C/D/E/F/G/H=334-501 |
| 1D01 | X-ray | 2.0 Å | A/B/C/D/E/F=334-501 |
| 1D0A | X-ray | 2.0 Å | A/B/C/D/E/F=334-501 |
| 1F3V | X-ray | 2.0 Å | B=331-501 |
| 1CA4 | X-ray | 2.2 Å | A/B/C/D/E/F=334-501 |
| 1CA9 | X-ray | 2.3 Å | A/B/C/D/E/F=310-501 |
| 1QSC | X-ray | 2.4 Å | A/B/C=311-501 |
| 1D0J | X-ray | 2.5 Å | A/B/C/D/E/F=334-501 |
| 3M0A | X-ray | 2.61 Å | A/B/C=266-329 |
| 3M06 | X-ray | 2.67 Å | A/B/C/D/E/F=266-329 |
| 1CZZ | X-ray | 2.7 Å | A/B/C=315-501 |
| 3M0D | X-ray | 2.8 Å | A/B=266-329 |
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