Q5SSZ7: E3 ubiquitin-protein ligase ZNRF3 (Znrf3)

E3 ubiquitin-protein ligase ZNRF3 (Znrf3) is a 913-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q5SSZ7.

Gene
Znrf3
Organism
Mus musculus
Length
913 residues
Mean pLDDT
51.2
Model
AF-Q5SSZ7-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 51.2 (low 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 accurate12%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions67%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby restricting the size of the intestinal stem cell zone (PubMed:22575959, PubMed:22895187). Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification (By similarity)

Subunit structure

Interacts with LRP6, FZD4, FZD5, FZD6 and FZD8 (By similarity). Interacts with RSPO1; interaction promotes indirect interaction with LGR4 and membrane clearance of ZNRF3 (By similarity). Interacts with LMBR1L (PubMed:31073040)

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4CDJX-ray1.5 ÅA/B=53-205
4C86X-ray2.0 ÅA/B=53-205
4C8PX-ray2.1 ÅA=53-205
4C8CX-ray2.4 ÅA/B=53-205
4C9AX-ray2.4 ÅA/C=53-205
4C8FX-ray2.69 ÅA/B/C/D=53-205
4C8AX-ray2.7 ÅA/B/C=53-205
4C99X-ray2.8 ÅA/C=53-205
4CDKX-ray2.8 ÅA/B/C/D=53-205
4C9EX-ray3.0 ÅA/C/E/G=53-205
4UFSX-ray4.8 ÅC=53-205

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