E3 ubiquitin-protein ligase RNF31 (RNF31) is a 1072-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96EP0.
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The mean pLDDT of this model is 77.6 (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 | 34% |
| 70 to 90 | Confident: backbone generally right | 43% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684, PubMed:28481331). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684). Linear ubiquitination mediated by the LUBAC…
Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:28481331). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181). Associates with the TNF-R1…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6KC5 | X-ray | 1.54 Å | B=853-1072 |
| 4LJO | X-ray | 1.56 Å | A=853-1072 |
| 7V8F | X-ray | 1.66 Å | B=697-793 |
| 4P09 | X-ray | 1.7 Å | A=1-179 |
| 9B0B | X-ray | 1.7 Å | E/G=350-379 |
| 9B12 | X-ray | 1.81 Å | G/H/I/J=350-379 |
| 4OWF | X-ray | 2.0 Å | G=350-379 |
| 4OYK | X-ray | 2.0 Å | A/B=3-179 |
| 6SC5 | X-ray | 2.1 Å | A=697-1072 |
| 6SC8 | X-ray | 2.11 Å | A=697-1072 |
| 6KC6 | X-ray | 2.12 Å | A/C/E/G/I/K=853-1072 |
| 4LJP | X-ray | 2.15 Å | A=853-1072 |
| 6GZY | X-ray | 2.15 Å | A/B=853-1072 |
| 6SC6 | X-ray | 2.25 Å | A=697-1072 |
| 4P0A | X-ray | 2.3 Å | A/C=1-179 |
| 8Z30 | X-ray | 2.3 Å | A/B/C=4-179 |
| 7UYJ | X-ray | 2.32 Å | A/B=1-179 |
| 4JUY | X-ray | 2.4 Å | A/B=1-180 |
| 9B0Z | X-ray | 2.41 Å | E/F=350-379 |
| 4LJQ | X-ray | 2.45 Å | A/B/C/D=853-1072 |
Showing 20 of 36 experimental structures (best resolution first).
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