Tumor necrosis factor receptor superfamily member 10A (TNFRSF10A) is a 468-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00220.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 66.1 (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 | 31% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 43% |
What pLDDT means and how to read it
Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518, PubMed:38532423). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (PubMed:19090789). Promotes the activation of NF-kappa-B (PubMed:9430227)
Monomer (PubMed:26457518). Homooligomers and heterooligomers with TNFRSF10B (PubMed:19090789). Three TNFRSF10A molecules interact with the TNFSF10 homotrimer (PubMed:26457518). Can interact with TRADD and RIPK1. Interacts with ARAP1. In the absence of stimulation, interacts with BIRC2, DDX3X and GSK3B. The interaction with BIRC2 and DDX3X is further enhanced upon receptor stimulation and…
Cell membrane, Membrane raft, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5CIR | X-ray | 3.0 Å | E/F/G=125-232 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.