Alpha-parvin (PARVA) is a 372-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NVD7.
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The mean pLDDT of this model is 79.6 (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 | 48% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 12% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration. Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process…
Component of the heterotrimeric IPP (ILK-PINCH-PARVIN) complex composed of ILK, LIMS1/PINCH and PARVA; the complex binds to F-actin via the C-terminal tail of LIMS1 and the N-terminal region of PARVA, promoting F-actin filament bundling (PubMed:11331308, PubMed:12432066, PubMed:15284246, PubMed:15817463, PubMed:20005845, PubMed:30367047, PubMed:35259013). Formation of the IPP complex is…
Cell junction, focal adhesion, Cell membrane, Cytoplasm, cytoskeleton, Cytoplasm, myofibril, sarcomere, Z line
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2VZC | X-ray | 1.05 Å | A/B=242-372 |
| 9D5E | X-ray | 1.5 Å | B=248-372 |
| 9D5F | X-ray | 1.5 Å | B=248-372 |
| 9D5H | X-ray | 1.5 Å | B=248-372 |
| 9D5I | X-ray | 1.5 Å | B=248-372 |
| 9D5P | X-ray | 1.5 Å | B=248-372 |
| 9D5G | X-ray | 1.55 Å | BBBB=248-372 |
| 2VZG | X-ray | 1.8 Å | B=242-372 |
| 3KMU | X-ray | 1.8 Å | B=248-372 |
| 3REP | X-ray | 1.8 Å | B=248-372 |
| 6MIB | X-ray | 1.8 Å | B=248-372 |
| 3KMW | X-ray | 2.0 Å | B=248-372 |
| 2VZD | X-ray | 2.1 Å | A/B=242-372 |
| 2VZI | X-ray | 2.2 Å | B=242-372 |
| 9UIU | X-ray | 2.35 Å | A/B=90-243 |
| 2K2R | NMR | A=244-372 |
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