Vasodilator-stimulated phosphoprotein (VASP) is a 380-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50552.
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The mean pLDDT of this model is 69.8 (low 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 | 36% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 21% |
| Below 50 | Very low: often disordered regions | 32% |
What pLDDT means and how to read it
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets…
Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the…
Cytoplasm, Cytoplasm, cytoskeleton, Cell junction, focal adhesion, Cell junction, tight junction, Cell projection, lamellipodium membrane, Cell projection, filopodium membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1USE | X-ray | 1.3 Å | A=336-380 |
| 2PBD | X-ray | 1.5 Å | V=203-245 |
| 1USD | X-ray | 1.7 Å | A=336-380 |
| 2PAV | X-ray | 1.8 Å | V=199-214 |
| 3CHW | X-ray | 2.3 Å | V=199-214 |
| 8YVL | EM | 2.47 Å | A/B/C/D=337-379 |
| 8GAT | EM | 3.0 Å | A=337-375 |
| 8GAU | EM | 3.6 Å | A=337-375 |
| 1EGX | NMR | A=1-115 |
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