Transient receptor potential cation channel subfamily V member 1 (Trpv1) is a 838-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O35433.
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The mean pLDDT of this model is 71.4 (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 | 23% |
| 70 to 90 | Confident: backbone generally right | 46% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius (By similarity). Upon activation, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel…
Homotetramer (PubMed:15190102, PubMed:24305160, PubMed:24305161, PubMed:27281200). Interacts with PIRT (By similarity). May also form a heteromeric channel with TRPV3 (By similarity). Interacts with CALM, PRKCM and CSK (PubMed:12808128, PubMed:15084474, PubMed:15471852, PubMed:17582331). Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (PubMed:11418861). Interacts with the…
Postsynaptic cell membrane, Cell projection, dendritic spine membrane, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3SUI | X-ray | 1.95 Å | B=767-801 |
| 8U4D | EM | 2.2 Å | A/B/C/D=110-764 |
| 8U3A | EM | 2.3 Å | A/D=110-764 |
| 8U3C | EM | 2.3 Å | A/D=1-838 |
| 8U43 | EM | 2.4 Å | A/B/C/D=110-764 |
| 7L2P | EM | 2.6 Å | A/B/C/D=110-764 |
| 7L2H | EM | 2.63 Å | A/B/C/D=2-838 |
| 7LP9 | EM | 2.63 Å | A/B/C/D=1-838 |
| 2PNN | X-ray | 2.7 Å | A=101-364 |
| 9W4M | EM | 2.7 Å | A/B/C/D=1-838 |
| 7L2S | EM | 2.71 Å | A/B/C/D=110-764 |
| 7MZ5 | EM | 2.76 Å | A/B/C/D=2-838 |
| 9W4T | EM | 2.87 Å | A/B/C/D=1-838 |
| 7MZD | EM | 2.9 Å | A/B/C/D=110-764 |
| 8U3J | EM | 2.9 Å | A/B/C/D=197-753 |
| 7MZ6 | EM | 2.91 Å | A/B/C/D=110-764 |
| 5IRX | EM | 2.95 Å | A/B/C/D=110-764 |
| 8U30 | EM | 3.0 Å | A/B/C/D=1-838 |
| 7MZC | EM | 3.03 Å | A/B/C/D=110-764 |
| 7RQY | EM | 3.04 Å | A/B/C/D=1-838 |
Showing 20 of 66 experimental structures (best resolution first).
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