P46934: E3 ubiquitin-protein ligase NEDD4 (NEDD4)

E3 ubiquitin-protein ligase NEDD4 (NEDD4) is a 1319-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P46934.

Gene
NEDD4
Organism
Homo sapiens
Length
1319 residues
Mean pLDDT
53.3
Model
AF-P46934-F1 v6
Model created
1 Aug 2025
PDB structures
15

Explore in 3D Color by confidence AlphaFold DB UniProt

Model confidence (pLDDT)

The mean pLDDT of this model is 53.3 (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 right23%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions57%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Specifically ubiquitinates 'Lys-63' in target proteins (PubMed:19920177, PubMed:21399620, PubMed:23644597). Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes (By similarity). Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes (PubMed:21765395). Promotes ubiquitination of RAPGEF2 (PubMed:11598133).…

Subunit structure

Binds, in vitro, through the WW2 and WW3 domains, to neural isoforms of ENAH that contain the PPSY motif. Interacts with BEAN1, LITAF, RNF11, WBP1, WBP2, PMEPAI and PRRG2 (By similarity). Interacts with NDFIP1 and NDFIP2; this interaction activates the E3 ubiquitin-protein ligase and may induce its recruitment to exosomes (By similarity). Interacts with UBE2D2 (By similarity). Interaction with…

Subcellular location

Cytoplasm, Nucleus, Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4N7FX-ray1.1 ÅA/B=841-874
4N7HX-ray1.7 ÅA=840-872
3B7YX-ray1.8 ÅA/B=517-571
9H9OX-ray2.12 ÅA=938-1312
9H9TX-ray2.17 ÅA=938-1312
5C91X-ray2.44 ÅA=938-1312
2XBFX-ray2.5 ÅA=938-1319
4BBNX-ray2.51 ÅA=938-1319
2XBBX-ray2.68 ÅA/B=938-1319
4BE8X-ray3.0 ÅA=938-1319
5C7JX-ray3.0 ÅA/B=939-1319
2KPZNMRA=834-878
2KQ0NMRA=834-878
2M3ONMRW=838-877
5AHTNMRA=838-877

More AlphaFold highlights

About this viewer

MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.