Low-density lipoprotein receptor-related protein 6 (LRP6) is a 1613-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75581.
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The mean pLDDT of this model is 79.2 (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 | 51% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes (PubMed:11357136, PubMed:11448771, PubMed:15778503, PubMed:16341017, PubMed:16513652, PubMed:17326769, PubMed:17400545, PubMed:19107203, PubMed:19293931, PubMed:19801552, PubMed:28341812, PubMed:34896607). Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in various processes including retinal angiogenesis and bone formation (PubMed:11357136, PubMed:11448771, PubMed:15778503, PubMed:16341017, PubMed:16513652, PubMed:17326769, PubMed:17400545, PubMed:19107203, PubMed:19293931,…
Homodimer; disulfide-linked. Forms phosphorylated oligomer aggregates on Wnt-signaling. Forms a WNT-signaling complex formed of a WNT protein, a FZD protein and LRP5 or LRP6. Interacts (via the extracellular domain) with WNT1; the interaction is enhanced by prior formation of the Wnt/Fzd complex. Interacts (via the beta-propeller regions 3 and 4) with WNT3A. Interacts (via the beta-propeller…
Cell membrane, Endoplasmic reticulum, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3SOV | X-ray | 1.27 Å | A=20-326 |
| 7NAM | X-ray | 1.6 Å | A=20-326 |
| 8FFE | X-ray | 1.72 Å | A=20-631 |
| 3SOB | X-ray | 1.9 Å | B=20-335 |
| 3SOQ | X-ray | 1.9 Å | A=20-326 |
| 4A0P | X-ray | 1.9 Å | A=629-1244 |
| 8DVM | X-ray | 2.0 Å | A=631-1253 |
| 4NM5 | X-ray | 2.3 Å | C=1567-1575 |
| 4NM7 | X-ray | 2.3 Å | C=1602-1610 |
| 8DVL | X-ray | 2.5 Å | A=631-1253 |
| 5AIR | X-ray | 2.53 Å | A/B=1565-1575 |
| 8DVN | X-ray | 2.53 Å | A=631-1253 |
| 6H15 | X-ray | 2.6 Å | A/B=630-1244 |
| 9FIX | X-ray | 2.78 Å | A=1516-1526 |
| 3S2K | X-ray | 2.8 Å | A/B=630-1246 |
| 3S8Z | X-ray | 2.8 Å | A=629-1243 |
| 3S94 | X-ray | 2.8 Å | A/B=20-630 |
| 9FIW | X-ray | 2.82 Å | A=1516-1521 |
| 9FIY | X-ray | 2.88 Å | A=1521-1526 |
| 4DG6 | X-ray | 2.9 Å | A=20-635 |
Showing 20 of 27 experimental structures (best resolution first).
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