Q96QK1: Vacuolar protein sorting-associated protein 35 (VPS35)

Vacuolar protein sorting-associated protein 35 (VPS35) is a 796-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96QK1.

Gene
VPS35
Organism
Homo sapiens
Length
796 residues
Mean pLDDT
91.3
Model
AF-Q96QK1-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.3 (very high 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 accurate74%
70 to 90Confident: backbone generally right23%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions1%

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 CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo…

Subunit structure

Component of the heterotrimeric retromer cargo-selective complex (CSC), also decribed 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, Membrane, Endosome, Early endosome, Late endosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8R0JX-ray2.4 ÅC/D=476-780
8R02X-ray2.5 ÅC/D=476-780
5OSIX-ray2.52 ÅB/E/H/K=471-781
5F0JX-ray2.7 ÅA=14-470
5F0PX-ray2.78 ÅA=14-470
2R17X-ray2.8 ÅC/D=483-780
5F0KX-ray3.07 ÅA/B/C/D/E=14-470
5F0MX-ray3.1 ÅA=14-470
8RKSX-ray3.1 ÅB/D/F/H=471-781
5F0LX-ray3.2 ÅA=14-470
5OSHX-ray4.3 ÅB/E/H/K=482-780
7BLNEM8.9 ÅA/C=1-796
7BLOEM9.5 ÅA/C=12-363

More AlphaFold highlights

About this viewer

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