Q6PJ69: E3 ubiquitin-protein ligase TRIM65 (TRIM65)

E3 ubiquitin-protein ligase TRIM65 (TRIM65) is a 517-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6PJ69.

Gene
TRIM65
Organism
Homo sapiens
Length
517 residues
Mean pLDDT
84.0
Model
AF-Q6PJ69-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.0 (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 accurate53%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions10%

What pLDDT means and how to read it

Function

E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation (PubMed:28594402, PubMed:34512673). Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (PubMed:24778252). This ubiquitination results in the suppressed expression of miR-138-5p leading to increased autophagy (PubMed:31160576). Upon enteroviral infection, promotes 'Lys-63'-mediated ubiquitination activation of IFIH1/MDA5 leading to innate signaling cascade (PubMed:28594402). Mechanistically, selectively recognizes MDA5 filaments that occur on…

Subunit structure

Homo-multimerizes (PubMed:24778252). Interacts with ARRDC4 (PubMed:28594402)

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7JL4X-ray1.92 ÅA/B/C=312-502
7JL0EM4.3 ÅB=312-502
7JL2EM4.3 ÅB/D/F=312-502

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