Q06696: Vacuolar protein-sorting-associated protein 36 (VPS36)

Vacuolar protein-sorting-associated protein 36 (VPS36) is a 566-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q06696.

Gene
VPS36
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
566 residues
Mean pLDDT
77.6
Model
AF-Q06696-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 77.6 (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 accurate37%
70 to 90Confident: backbone generally right36%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions16%

What pLDDT means and how to read it

Function

Component of the ESCRT-II complex, which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs (PubMed:12194858, PubMed:15329733, PubMed:15469844). The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation (PubMed:12194858). The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex (PubMed:12194858). Involved in the trafficking of the plasma membrane ATPase (PubMed:12194858). Its ability to bind ubiquitin plays a central role in endosomal sorting of ubiquitinated cargo proteins by the ESCRT complexes (PubMed:15029239)

Subunit structure

Component of the endosomal sorting required for transport complex II (ESCRT-II), which consists of 2 copies of VPS25, 1 copy of SNF8, and 1 copy of VPS36 (PubMed:15329733, PubMed:15469844). The ESCRT-II complex interacts directly with the VPS20 subunit of the ESCRT-III complex (PubMed:12194858). Binds ubiquitin (PubMed:15029239)

Subcellular location

Cytoplasm, Endosome membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2CAYX-ray1.9 ÅA/B=1-103
2J9UX-ray2.0 ÅB/D=110-171
1U5TX-ray3.6 ÅB=396-564
1W7PX-ray3.6 ÅD=1-566

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