Q13114: TNF receptor-associated factor 3 (TRAF3)

TNF receptor-associated factor 3 (TRAF3) is a 568-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13114.

Gene
TRAF3
Organism
Homo sapiens
Length
568 residues
Mean pLDDT
87.9
Model
AF-Q13114-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.9 (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 accurate71%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions6%

What pLDDT means and how to read it

Function

Cytoplasmic E3 ubiquitin ligase that regulates various signaling pathways, such as the NF-kappa-B, mitogen-activated protein kinase (MAPK) and interferon regulatory factor (IRF) pathways, and thus controls a lot of biological processes in both immune and non-immune cell types (PubMed:33148796, PubMed:33608556). In TLR and RLR signaling pathways, acts as an E3 ubiquitin ligase promoting the synthesis of 'Lys-63'-linked polyubiquitin chains on several substrates such as ASC that lead to the activation of the type I interferon response or the inflammasome (PubMed:25847972, PubMed:27980081). Following the activation of certain TLRs such as TLR4, acts as a negative NF-kappa-B regulator,…

Subunit structure

Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts with LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14, TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and IFT54. Interaction with TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the same binding site. Interacts with TICAM1. Interacts with TRAFD1. Interacts with OTUB1,…

Subcellular location

Cytoplasm, Endosome, Mitochondrion

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8T5PX-ray2.5 ÅA/B/C/D/E/F=377-568
2GKWX-ray2.7 ÅA=377-568
1FLKX-ray2.8 ÅA/B=341-568
1ZMSX-ray2.8 ÅA=377-568
8ZUKEM2.83 ÅA/B/C/G/H/I/M/N/O/S/T/U/Y/Z/a/e/f/g/k/l/m=267-568
1L0AX-ray2.9 ÅA=377-568
1FLLX-ray3.5 ÅA/B=341-568
1KZZX-ray3.5 ÅA=377-568
1RF3X-ray3.5 ÅA=377-568
2ECYNMRA=43-101

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