Vacuolar protein sorting-associated protein 29 (VPS29) is a 182-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBQ0.
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The mean pLDDT of this model is 96.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 98% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the commander complex is composed of the CCC subcomplex and the retriever subcomplex (PubMed:37172566, PubMed:39587083, PubMed:38062209, PubMed:38459129). Component of the retriever complex, which is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:28892079, PubMed:37172566, PubMed:39587083, PubMed:38062209, PubMed:38459129). Component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional…
Component of the commander complex consisting of the CCC subcomplex and the retriever subcomplex (PubMed:37172566, PubMed:28892079, PubMed:39587083, PubMed:38062209, PubMed:38459129). Component of the heterotrimeric retriever complex formed by VPS26C, VPS29 and VPS35L; within the complex interacts with VPS35L (PubMed:37172566, PubMed:28892079, PubMed:31712251, PubMed:39587083, PubMed:38062209,…
Cytoplasm, Membrane, Endosome membrane, Early endosome, Late endosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8ESE | X-ray | 1.35 Å | Z=1-182 |
| 5GTU | X-ray | 1.5 Å | A=2-182 |
| 6XS7 | X-ray | 1.58 Å | A=1-182 |
| 6XSA | X-ray | 1.83 Å | A=1-182 |
| 6XS5 | X-ray | 2.01 Å | A=1-182 |
| 1W24 | X-ray | 2.1 Å | A=1-182 |
| 8R0J | X-ray | 2.4 Å | A/B=1-182 |
| 5WYH | X-ray | 2.46 Å | A/C=2-182 |
| 8R02 | X-ray | 2.5 Å | A/B=1-182 |
| 5OSI | X-ray | 2.52 Å | A/D/G/J=1-182 |
| 6XS9 | X-ray | 2.69 Å | A/B=1-182 |
| 2R17 | X-ray | 2.8 Å | A/B=1-182 |
| 8SYN | EM | 2.94 Å | B=2-182 |
| 8SYO | EM | 2.94 Å | B=2-182 |
| 8RKS | X-ray | 3.1 Å | A/C/E/G=1-182 |
| 8SYM | EM | 3.2 Å | B=2-182 |
| 9AU7 | EM | 3.4 Å | B=2-182 |
| 5OSH | X-ray | 4.3 Å | A/D/G/J=1-182 |
| 8P0V | EM | 6.5 Å | N=1-182 |
| 8P0X | EM | 7.5 Å | N=1-182 |
Showing 20 of 21 experimental structures (best resolution first).
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