Transitional endoplasmic reticulum ATPase (VCP) is a 806-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P55072.
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The mean pLDDT of this model is 82.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 42% |
| 70 to 90 | Confident: backbone generally right | 43% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 7% |
What pLDDT means and how to read it
Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex…
Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1,…
Cytoplasm, cytosol, Endoplasmic reticulum, Nucleus, Cytoplasm, Stress granule
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5B6C | X-ray | 1.55 Å | A=21-191 |
| 7PUX | X-ray | 1.73 Å | A=1-460 |
| 3TIW | X-ray | 1.8 Å | A/B=1-187 |
| 4KDL | X-ray | 1.81 Å | A=21-196 |
| 4KDI | X-ray | 1.86 Å | A/B=21-196 |
| 5EPP | X-ray | 1.88 Å | A=21-199 |
| 3EBB | X-ray | 1.9 Å | E/F/G/H=797-806 |
| 6G2V | X-ray | 1.9 Å | A=462-764 |
| 6G2Z | X-ray | 1.92 Å | A=462-764 |
| 4KO8 | X-ray | 1.98 Å | A/B=1-481 |
| 3QQ8 | X-ray | 2.0 Å | A=2-187 |
| 3QWZ | X-ray | 2.0 Å | A=1-208 |
| 6G2X | X-ray | 2.08 Å | A=462-764 |
| 10QQ | EM | 2.13 Å | A/B/C/D/E/F/G/H/I/J/K/L=1-806 |
| 6G2Y | X-ray | 2.15 Å | A=462-764 |
| 3HU3 | X-ray | 2.2 Å | A/B=1-481 |
| 3QC8 | X-ray | 2.2 Å | A=21-196 |
| 5DYG | X-ray | 2.2 Å | A=1-460 |
| 5GLF | X-ray | 2.25 Å | A/C/E/G=21-199 |
| 10QR | EM | 2.3 Å | A/B/C/D/E/F=1-806 |
Showing 20 of 143 experimental structures (best resolution first).
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