Q96PU5: E3 ubiquitin-protein ligase NEDD4-like (NEDD4L)

E3 ubiquitin-protein ligase NEDD4-like (NEDD4L) is a 975-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96PU5.

Gene
NEDD4L
Organism
Homo sapiens
Length
975 residues
Mean pLDDT
68.4
Model
AF-Q96PU5-F1 v6
Model created
1 Aug 2025
PDB structures
20

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.4 (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 accurate29%
70 to 90Confident: backbone generally right29%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions32%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins and is thereby implicated in the regulation of various signaling pathways including autophagy, innate immunity or DNA repair (PubMed:20064473, PubMed:31959741, PubMed:33608556). Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation (PubMed:15496141). Down-regulates autophagy and cell growth by ubiquitinating and reducing cellular ULK1 or ASCT2 levels (PubMed:28820317, PubMed:31959741). Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, SCN2A/Nav1.2, SCN3A/Nav1.3, SCN5A/Nav1.5,…

Subunit structure

Interacts with UBE2E3 (By similarity). Interacts with NDFIP1; this interaction activates the E3 ubiquitin-protein ligase (PubMed:11748237, PubMed:26363003). Interacts with NDFIP2; this interaction activates the E3 ubiquitin-protein ligase (PubMed:26363003). Interacts (via WW domains) with SCN1A (By similarity). Interacts (via WW domains) with SCN2A (PubMed:15548568). Interacts (via WW domains)…

Subcellular location

Cytoplasm, Golgi apparatus, Endosome, multivesicular body

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7LP1X-ray1.35 ÅA=494-532
7LP3X-ray1.61 ÅA/C=193-226
6ZBTX-ray1.8 ÅE/F/G/H=338-347
2NSQX-ray1.85 ÅA=1-154
7LP2X-ray1.88 ÅA/C/E=385-418
6ZC9X-ray1.9 ÅE/F/G/H=444-453
2ONIX-ray2.2 ÅA=594-967
7NMZX-ray2.3 ÅC=335-455
5HPKX-ray2.43 ÅA=594-975
9Z5QEM3.06 ÅB=541-975
3JW0X-ray3.1 ÅC/D=596-975
3JVZX-ray3.3 ÅC/D=596-975
9GIKEM3.58 ÅA=1-975
9GIMEM4.11 ÅA=1-975
2LAJNMRA=496-535
2LB2NMRA=386-420
2LTYNMRA=385-417
2MPTNMRA=496-539, B=945-957
7LP4NMRA=493-539
7LP5NMRA=493-539

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