Vacuolar transporter chaperone complex subunit 4 (VTC4) is a 721-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P47075.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 81.2 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 42% |
| 70 to 90 | Confident: backbone generally right | 41% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:19390046, PubMed:25315834). PolyP synthesis is tightly coupled…
The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1-VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear…
Vacuole membrane, Cytoplasm, cell cortex, Endoplasmic reticulum membrane, Cytoplasmic vesicle, autophagosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3G3T | X-ray | 1.85 Å | A=189-480 |
| 3G3R | X-ray | 2.0 Å | A/B=189-480 |
| 3G3U | X-ray | 2.07 Å | A/B=189-480 |
| 5IIT | X-ray | 2.13 Å | A/B/C/D=1-178 |
| 3G3Q | X-ray | 2.64 Å | A/B=189-480 |
| 5IIG | X-ray | 2.99 Å | A=2-480 |
| 7YTJ | EM | 3.0 Å | D=2-721 |
| 5IIQ | X-ray | 3.03 Å | A=2-480 |
| 9UMG | EM | 3.04 Å | D=196-721 |
| 8I6V | EM | 3.06 Å | E=1-721 |
| 5LNC | X-ray | 3.29 Å | A/B=1-178 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.