E3 ubiquitin-protein ligase TRIM21 (Trim21) is a 470-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q62191.
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The mean pLDDT of this model is 89.4 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 68% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2 (By similarity). Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination (By similarity). Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes (By similarity). A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome (By similarity). Monoubiquitinates IKBKB that will negatively…
Homotrimer (By similarity). Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts with CALR, CUL1, FBXW11, HSPA5, IKBKB, IRF3, SKP1 and VCP. Interacts with SKP2; the interaction with SKP2 does not depend on an intact F-box domain. Interacts (via N-terminus and C-terminus) with DCP2 (via N-terminus and C-terminus) (By similarity). Interacts (via C-terminus) with…
Cytoplasm, Cytoplasmic vesicle, autophagosome, Nucleus, Cytoplasm, P-body, Cytoplasm, Stress granule
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7HLL | X-ray | 1.15 Å | B=291-470 |
| 7HLM | X-ray | 1.15 Å | B=291-470 |
| 7HLO | X-ray | 1.15 Å | B=291-470 |
| 7HLS | X-ray | 1.15 Å | B=291-470 |
| 7HLT | X-ray | 1.15 Å | B=291-470 |
| 7HLU | X-ray | 1.15 Å | B=291-470 |
| 7HM2 | X-ray | 1.15 Å | B=291-470 |
| 7HMA | X-ray | 1.15 Å | B=291-470 |
| 7HMP | X-ray | 1.15 Å | B=291-470 |
| 7HMR | X-ray | 1.15 Å | B=291-470 |
| 7HMS | X-ray | 1.15 Å | B=291-470 |
| 7HMU | X-ray | 1.15 Å | B=291-470 |
| 7HMV | X-ray | 1.15 Å | B=291-470 |
| 7HMY | X-ray | 1.15 Å | B=291-470 |
| 7HNC | X-ray | 1.15 Å | B=291-470 |
| 7HNU | X-ray | 1.15 Å | B=291-470 |
| 7HNZ | X-ray | 1.15 Å | B=291-470 |
| 7HO0 | X-ray | 1.15 Å | B=291-470 |
| 7HO2 | X-ray | 1.15 Å | B=291-470 |
| 7HOB | X-ray | 1.15 Å | B=291-470 |
Showing 20 of 113 experimental structures (best resolution first).
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