Vimentin (VIM) is a 466-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08670.
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The mean pLDDT of this model is 77.1 (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 | 50% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). May promote axon outgrowth and motor fiber repair via DSP-mediated recruitment to outgrowth tips (By similarity)
Homomer assembled from elementary dimers (PubMed:20176112). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Identified in a complex containing at least DSP, JUP, VIM and CDH2; the complex is more abundant following crush injury in regenerating motor neurons and may promote axon outgrowth and motor fiber repair (By similarity).…
Cytoplasm, Cytoplasm, cytoskeleton, Nucleus matrix, Cell membrane, Cell projection, axon
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1GK7 | X-ray | 1.4 Å | A=101-138 |
| 4YPC | X-ray | 1.44 Å | A=161-243 |
| 4MD5 | X-ray | 1.65 Å | C=66-78 |
| 3SWK | X-ray | 1.7 Å | A/B=153-238 |
| 4MDJ | X-ray | 1.7 Å | C=66-78 |
| 3G1E | X-ray | 1.83 Å | A/B=102-138 |
| 1GK6 | X-ray | 1.9 Å | A/B=385-412 |
| 6ATF | X-ray | 1.9 Å | C/F=59-71 |
| 6ATI | X-ray | 1.98 Å | C/F=59-71 |
| 4MDI | X-ray | 2.0 Å | C=66-78 |
| 4YV3 | X-ray | 2.0 Å | A/B/C=161-238 |
| 6YXK | X-ray | 2.0 Å | C=59-74 |
| 4MD0 | X-ray | 2.19 Å | C=59-71 |
| 5WHF | X-ray | 2.25 Å | A/B/C/D/E/F/G/H=153-238 |
| 1GK4 | X-ray | 2.3 Å | A/B/C/D/E/F=328-411 |
| 3TRT | X-ray | 2.3 Å | A/B=261-335 |
| 4MCY | X-ray | 2.3 Å | C=66-78 |
| 6BIR | X-ray | 2.3 Å | C=419-431 |
| 4MCZ | X-ray | 2.41 Å | C=59-71 |
| 3S4R | X-ray | 2.45 Å | A/B=99-189 |
Showing 20 of 26 experimental structures (best resolution first).
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