P09493: Tropomyosin alpha-1 chain (TPM1)

Tropomyosin alpha-1 chain (TPM1) is a 284-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09493.

Gene
TPM1
Organism
Homo sapiens
Length
284 residues
Mean pLDDT
91.6
Model
AF-P09493-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate75%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Binds to actin filaments in muscle and non-muscle cells (PubMed:23170982). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:23170982). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments

Subunit structure

Homodimer (PubMed:23170982). Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a beta (TPM2) chain (By similarity). Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG (By similarity). Interacts (via N-terminus) with LMOD2 (via N-terminus) and TMOD1 (via N-terminus) (PubMed:26873245)

Subcellular location

Cytoplasm, cytoskeleton

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5KHTX-ray1.5 ÅA/B/C/D=1-28
3MUDX-ray2.2 ÅC/D=1-29
9ZBLEM2.79 ÅM/N/O/P=1-284
9ZBPEM3.12 ÅM/N/O/P=1-284
8ZB7EM3.19 ÅL/N/O/P=45-210
8EFHEM3.3 ÅO/P=1-284
8EFIEM3.4 ÅO/P=1-284
8ENCEM3.6 ÅO/P=1-284
6X5ZEM4.24 ÅO/P=1-284
6KN8EM4.8 ÅP/Q/W/X=11-284, R/S/Y/Z=1-29
7UTIEM4.8 ÅW/b/e/f/g/h/i/j=1-284
6KN7EM6.6 ÅP/Q/W/X=11-284, R/S/Y/Z=1-29
7UTLEM6.6 ÅW/Z/a/b/g/h/i/j=1-284
6UT2NMRB/C=1-14

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