Tropomyosin alpha-1 chain (Tpm1) is a 284-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P58771.
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The mean pLDDT of this model is 91.6 (very high 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 | 75% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments
Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG. Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1 (via N-terminus)
Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8ZBN | EM | 3.02 Å | R/S/T/U=93-270 |
| 9E2E | EM | 4.0 Å | G/H/I/J/L/M/N/O=1-284 |
| 8ZBK | EM | 4.28 Å | R/S/T/U=93-270 |
| 9MOW | EM | 4.9 Å | L/M/N/O=1-284 |
| 9MOP | EM | 5.0 Å | K/L/M/N=1-284 |
| 9MOM | EM | 5.1 Å | L/M/N/O=1-284 |
| 9MO7 | EM | 5.2 Å | K/L/M/N=1-284 |
| 9MO8 | EM | 5.2 Å | L/M/N/O=1-284 |
| 9MOL | EM | 5.2 Å | L/M/N/O=1-284 |
| 9MON | EM | 5.2 Å | L/M/N/O=1-284 |
| 9MOO | EM | 5.2 Å | K/L/M/N=1-284 |
| 9MOX | EM | 5.2 Å | K/L/M/N=1-284 |
| 9MO4 | EM | 5.3 Å | K/L/M/N=1-284 |
| 9MO5 | EM | 5.3 Å | K/L/M/N=1-284 |
| 9MO6 | EM | 5.3 Å | K/L/M/N=1-284 |
| 9MOA | EM | 5.4 Å | K/L/M/N=1-284 |
| 9MOI | EM | 5.4 Å | K/L/M/N=1-284 |
| 9MOB | EM | 5.5 Å | L/M/N/O=1-284 |
| 9MO9 | EM | 5.6 Å | K/L/M/N=1-284 |
| 9MOC | EM | 5.6 Å | L/M/N/O=1-284 |
Showing 20 of 25 experimental structures (best resolution first).
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