Q15628: Tumor necrosis factor receptor type 1-associated DEATH domain protein (TRADD)

Tumor necrosis factor receptor type 1-associated DEATH domain protein (TRADD) is a 312-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15628.

Gene
TRADD
Organism
Homo sapiens
Length
312 residues
Mean pLDDT
83.3
Model
AF-Q15628-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate60%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD (PubMed:23955153, PubMed:7758105, PubMed:8612133). Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B (PubMed:7758105, PubMed:8612133). The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity)

Subunit structure

Stimulation of TNF receptor TNFRSF1A leads to the formation of two distinct signaling complexes (PubMed:14585990, PubMed:21307340, PubMed:7758105, PubMed:8612133). Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:14585990, PubMed:21307340,…

Subcellular location

Nucleus, Cytoplasm, Cytoplasm, cytoskeleton

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6AC0X-ray1.45 ÅA=195-312
1F3VX-ray2.0 ÅA=1-179
9VGDEM3.3 ÅA/B/C/E/F/H/I/J/K/M/N/Q/R/S/T/V/W/Y/Z/b/c/e/f/g/h/j/k/l=199-312
9VINEM3.41 ÅE/F/N/V/W=199-312
1F2HNMRA=1-169
5XMENMRA=199-312
7CSQNMRB=199-312

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