Ubiquitin-conjugating enzyme E2 L3 (UBE2L3) is a 154-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P68036.
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The mean pLDDT of this model is 95.6 (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 | 94% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine; in contrast, it has activity with the RBR family E3 enzymes, such as PRKN, RNF31 and ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates ubiquitination by the CUL9-RBX1 complex (PubMed:38605244). In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated…
Interacts with PRKN; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A; used by the papilloma virus HPV-16 E6 protein to ubiquitinate p53/TP53. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7V8F | X-ray | 1.66 Å | A=1-154 |
| 4Q5E | X-ray | 1.87 Å | C=1-154 |
| 4Q5H | X-ray | 2.0 Å | C=1-154 |
| 1C4Z | X-ray | 2.6 Å | D=1-154 |
| 5HPT | X-ray | 2.84 Å | C/F=2-154 |
| 1FBV | X-ray | 2.9 Å | C=1-154 |
| 6CP2 | X-ray | 2.9 Å | B=1-154 |
| 8EB0 | X-ray | 3.03 Å | B=1-154 |
| 8EAZ | X-ray | 3.08 Å | C/D=1-154 |
| 5UDH | X-ray | 3.24 Å | C/D=1-154 |
| 3SY2 | X-ray | 3.27 Å | C/D=1-154 |
| 3SQV | X-ray | 3.3 Å | C/D=1-154 |
| 5TTE | X-ray | 3.5 Å | E=1-154 |
| 7OIK | EM | 3.5 Å | B=1-154 |
| 7B5N | EM | 3.6 Å | D=1-154 |
| 6DJW | X-ray | 3.8 Å | C=1-154 |
| 7B5L | EM | 3.8 Å | D=1-154 |
| 9I1J | EM | 3.8 Å | B=1-154 |
| 6DJX | X-ray | 4.8 Å | C=1-154 |
| 6N13 | NMR | C=1-154 |
Showing 20 of 21 experimental structures (best resolution first).
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