E3 ubiquitin-protein ligase TRIM21 (TRIM21) is a 475-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P19474.
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The mean pLDDT of this model is 90.7 (very high 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 | 77% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2 (PubMed:16297862, PubMed:16316627, PubMed:16472766, PubMed:16880511, PubMed:18022694, PubMed:18361920, PubMed:18641315, PubMed:18845142, PubMed:19675099, PubMed:26347139). 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 (PubMed:16880511, PubMed:19675099). Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes (PubMed:16880511). A TRIM21-containing SCF(SKP2)-like complex is shown to mediate…
Homotrimer (PubMed:17156811, PubMed:26347139). Interacts (via C-terminus) with IRF8 (via C-terminus) (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)…
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 |
|---|---|---|---|
| 9QBA | X-ray | 1.45 Å | A=287-465 |
| 9II5 | X-ray | 1.49 Å | A=287-461 |
| 8Y58 | X-ray | 1.6 Å | A=287-475 |
| 8Y5B | X-ray | 1.74 Å | A=287-475 |
| 8Y59 | X-ray | 1.89 Å | A=287-475 |
| 5OLM | X-ray | 1.95 Å | A/B=1-129 |
| 9M3N | X-ray | 2.08 Å | A=285-464 |
| 9EK5 | X-ray | 2.1 Å | A=288-465 |
| 9Q9P | X-ray | 2.1 Å | B=287-475 |
| 7BBD | X-ray | 2.2 Å | B=1-85 |
| 8A58 | X-ray | 2.25 Å | C/D=1-85 |
| 9Q9Q | X-ray | 2.25 Å | A/B=287-475 |
| 9Q9R | X-ray | 2.33 Å | B=287-475 |
| 2IWG | X-ray | 2.35 Å | B/E=287-465 |
| 9Q9O | X-ray | 2.46 Å | A/B/C/D=287-475 |
| 6S53 | X-ray | 2.8 Å | A/B/G/H=1-85 |
| 6FGA | X-ray | 2.82 Å | A/B/C/D/E/F/G/H=1-98 |
| 5JPX | NMR | A=86-130 |
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