Q8ND25: E3 ubiquitin-protein ligase ZNRF1 (ZNRF1)

E3 ubiquitin-protein ligase ZNRF1 (ZNRF1) is a 227-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8ND25.

Gene
ZNRF1
Organism
Homo sapiens
Length
227 residues
Mean pLDDT
67.0
Model
AF-Q8ND25-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.0 (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 accurate32%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution35%
Below 50Very low: often disordered regions28%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that plays a role in different processes including cell differentiation, receptor recycling or regulation of inflammation (PubMed:28593998, PubMed:33996800, PubMed:37158982). Mediates the ubiquitination of AKT1 and GLUL, thereby playing a role in neuron cells differentiation. Plays a role in the establishment and maintenance of neuronal transmission and plasticity. Regulates Schwann cells differentiation by mediating ubiquitination of GLUL. Promotes neurodegeneration by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of AKT1 in axons: degradation of AKT1 prevents AKT1-mediated phosphorylation of GSK3B, leading to GSK3B activation and…

Subunit structure

Interacts with AKT1, GLUL and TUBB2A (By similarity). Interacts with ZNRF2 (PubMed:22797923). Interacts (via its RING domain) with UBE2N (PubMed:29626159). Interacts (when phosphorylated) with YWHAE (PubMed:22797923)

Subcellular location

Endosome, Lysosome, Membrane, Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5YWRX-ray1.47 ÅB=139-227

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