Q0PF16: Tripartite motif-containing protein 5 (TRIM5)

Tripartite motif-containing protein 5 (TRIM5) is a 497-residue protein from Macaca mulatta. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q0PF16.

Gene
TRIM5
Organism
Macaca mulatta
Length
497 residues
Mean pLDDT
85.1
Model
AF-Q0PF16-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.1 (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 accurate54%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the…

Subunit structure

Can form homodimers and homotrimers. In addition to lower-order dimerization, also exhibits a higher-order multimerization and both low- and high-order multimerizations are essential for its restriction activity. Interacts with MAP3K7/TAK1, TAB2 and TAB3 (By similarity). Interacts with HSPA8/HSC70, PSMC2, PSMC4, PSMC5 and PSMD7 (PubMed:20053985, PubMed:22078707). Interacts with SQSTM1…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3UV9X-ray1.55 ÅA=292-497
5K3QX-ray1.8 ÅA/B/C/D=94-154, A/B/C/D=229-261
5EIUX-ray1.91 ÅA/D=89-159, A/D=226-265
4TKPX-ray2.08 ÅB=2-92
5F7TX-ray2.29 ÅE/F/H/L=89-159, E/F/H/L=226-265
5W9AX-ray2.74 ÅA/B=95-287
5IEAX-ray3.26 ÅA/B/C/D/F/K=89-159, A/B/C/D/F/K=226-265
4B3NX-ray3.3 ÅA/B=275-493
2LM3NMRA=292-497

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