O75436: Vacuolar protein sorting-associated protein 26A (VPS26A)

Vacuolar protein sorting-associated protein 26A (VPS26A) is a 327-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75436.

Gene
VPS26A
Organism
Homo sapiens
Length
327 residues
Mean pLDDT
87.7
Model
AF-O75436-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.7 (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 accurate73%
70 to 90Confident: backbone generally right17%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Acts as a component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The…

Subunit structure

Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35 (PubMed:11102511, PubMed:28892079). The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform (By similarity). The CSC is believed to…

Subcellular location

Cytoplasm, Endosome membrane, Early endosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2FAUX-ray2.1 ÅA=1-327
5F0JX-ray2.7 ÅB=2-326
5F0PX-ray2.78 ÅB=1-321
5F0MX-ray3.1 ÅB=1-321
5F0LX-ray3.2 ÅB=1-317
7BLOEM9.5 ÅF/J=8-301

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