Q63HN8: E3 ubiquitin-protein ligase RNF213 (RNF213)

E3 ubiquitin-protein ligase RNF213 (RNF213) is a 557-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q63HN8.

Gene
RNF213
Organism
Homo sapiens
Length
557 residues
Mean pLDDT
86.3
Model
AF-Q63HN8-6-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.3 (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 accurate45%
70 to 90Confident: backbone generally right45%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:21799892, PubMed:26126547, PubMed:26278786, PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115, PubMed:39375464). Also acts indirectly by mediating the…

Subunit structure

Monomer (By similarity). Oligomerates upon ISGylation induced by type I interferon (PubMed:34599178). Interacts with UBE2L3/UBCH7; UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for the ubiquitin ligase activity (By similarity). Interacts with UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849)

Subcellular location

Cytoplasm, cytosol, Lipid droplet

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9JTAX-ray1.7 ÅC=3990-4056
8S24EM3.0 ÅA=1-5207
9G08EM3.3 ÅA=1-5207
9G09EM3.4 ÅA=1-5207

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