O60493: Sorting nexin-3 (SNX3)

Sorting nexin-3 (SNX3) is a 162-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60493.

Gene
SNX3
Organism
Homo sapiens
Length
162 residues
Mean pLDDT
88.8
Model
AF-O60493-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.8 (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 accurate64%
70 to 90Confident: backbone generally right29%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (PubMed:21725319,…

Subunit structure

Interacts with VPS26A, VPS29 and VPS35; the interaction with VPS35 is direct. The association with the retromer CSC subcomplex subunits is proposed to represent a functional distinct retromer variant described as SNX3-retromer complex (PubMed:21725319, PubMed:24344282, PubMed:30213940). Interacts with USP10 and SCNN1A (By similarity). Interacts with TRFC (By similarity). Interacts with SNX8; 2…

Subcellular location

Early endosome, Cytoplasmic vesicle, phagosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2YPSX-ray2.6 ÅA/B/C/D=24-155
5F0JX-ray2.7 ÅC=1-162
5F0PX-ray2.78 ÅC=1-162
5F0MX-ray3.1 ÅC=1-162
5F0LX-ray3.2 ÅC=1-162
7BLOEM9.5 ÅG/L=4-158
2MXCNMRA=2-162

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