Transient receptor potential cation channel subfamily V member 5 (Trpv5) is a 730-residue protein from Oryctolagus cuniculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9XSM3.
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The mean pLDDT of this model is 83.2 (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 | 60% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine (PubMed:10085067, PubMed:11035011, PubMed:12574114, PubMed:29323279). Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (By similarity). The channel is activated by low internal calcium level and the current exhibits an inward rectification (PubMed:29323279). A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay (PubMed:11035011). Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (PubMed:12574114)
Homotetramer (PubMed:29323279). Probably forms heterotetramers with TRPV6 (PubMed:12574114). Interacts with TRPV6 (PubMed:12574114). Interacts with S100A10 and probably with the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is required for the trafficking to the plasma membrane. Interacts with calmodulin. Interacts with BSPRY, which results in its inactivation
Cell membrane, Apical cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8TF2 | EM | 2.57 Å | A/B/C/D=1-730 |
| 7T6O | EM | 2.6 Å | A/B/C/D=1-730 |
| 8FFQ | EM | 2.65 Å | A/B/C/D=1-730 |
| 6O1U | EM | 2.8 Å | A/B/C/D=1-730 |
| 7T6M | EM | 2.8 Å | A/B/C/D=1-730 |
| 7T6P | EM | 2.8 Å | A/B/C/D=1-730 |
| 8TF4 | EM | 2.86 Å | A/B/C/D=1-730 |
| 6O1N | EM | 2.9 Å | A/B/C/D=1-730 |
| 7T6N | EM | 2.9 Å | A/B/C/D=1-730 |
| 8TF3 | EM | 2.94 Å | A/B/C/D=1-730 |
| 8FFN | EM | 2.96 Å | A/B/C/D=1-730 |
| 6O1P | EM | 3.0 Å | A/B/C/D=1-730 |
| 7T6K | EM | 3.0 Å | A/B/C/D=1-730 |
| 7T6R | EM | 3.0 Å | A/B/C/D=1-730 |
| 8FHH | EM | 3.09 Å | A/B/C/D=1-730 |
| 7T6J | EM | 3.2 Å | A/B/C/D=1-730 |
| 8FHI | EM | 3.25 Å | A/B/C/D=1-730 |
| 6O20 | EM | 3.3 Å | A/B/C/D/E=1-730 |
| 9O6G | EM | 3.37 Å | A/B/C/D=1-730 |
| 7T6Q | EM | 3.4 Å | A/B/C/D=1-730 |
Showing 20 of 28 experimental structures (best resolution first).
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