LRP6_E1 in complex with Lr-EET-3.5. Determined by X-ray diffraction at 1.6 Å resolution. Released 29 Jun 2022.
Explore 7NAM in 3D Show helices and sheets RCSB PDB PDBe
7NAM contains 7 α-helices and 31 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-26 | 5 | 1 |
| β-strand | 28-35 | 8 | 1 |
| α-helix | 42-43 | 2 | |
| β-strand | 44-59 | 16 | 1 |
| α-helix | 60-62 | 3 | |
| β-strand | 64-69 | 6 | 1 |
| β-strand | 74-79 | 6 | 1 |
| β-strand | 88-92 | 5 | 1 |
| β-strand | 99-103 | 5 | 2 |
| β-strand | 108-113 | 6 | 2 |
| β-strand | 118-123 | 6 | 2 |
| β-strand | 130-133 | 4 | 2 |
| β-strand | 140-146 | 7 | 3 |
| β-strand | 151-156 | 6 | 3 |
| β-strand | 162-167 | 6 | 3 |
| β-strand | 174-177 | 4 | 3 |
| β-strand | 184-190 | 7 | 4 |
| β-strand | 195-200 | 6 | 4 |
| β-strand | 205-209 | 5 | 4 |
| β-strand | 217-220 | 4 | 4 |
| β-strand | 227-233 | 7 | 5 |
| β-strand | 236-241 | 6 | 5 |
| β-strand | 246-251 | 6 | 5 |
| β-strand | 259-262 | 4 | 5 |
| β-strand | 271-274 | 4 | 1 |
| α-helix | 276-278 | 3 | |
| α-helix | 290-292 | 3 | |
| β-strand | 296-299 | 4 | 6 |
| β-strand | 306-309 | 4 | 6 |
| α-helix | 314-315 | 2 | |
| β-strand | 316 | 1 | 7 |
| α-helix | 317 | 1 | |
| β-strand | 323 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12 | 1 | 8 |
| α-helix | 16-18 | 3 | |
| β-strand | 25 | 1 | 9 |
| β-strand | 30 | 1 | 8 |
| β-strand | 31 | 1 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Low-density lipoprotein receptor-related protein 6 | A | protein | 317 | Homo sapiens | O75581 (AlphaFold model) |
| Trypsin inhibitor 2 | B | protein | 32 | synthetic construct |
>7NAM_1 Low-density lipoprotein receptor-related protein 6 (chains A) GSAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFSHGLIYWSDVSEEAIKR TEFNKTESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQEL DQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFIIINSEIYWPNGLTLDYEEQKLY WADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDILYWTDWSTHSILACNKYTGEG LREIHSDIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLL ENGKTCKDGNSHHHHHH
>7NAM_2 Trypsin inhibitor 2 (chains B) GCQSNHILKHNRCKQDSDCLAGCVCGPNGFCG
Directed evolution identifies high-affinity cystine-knot peptide agonists and antagonists of Wnt/ beta-catenin signaling. Hansen, S., Zhang, Y., Hwang, S. et al. Proc Natl Acad Sci U S A (2022) 119:e2207327119-e2207327119. DOI 10.1073/pnas.2207327119 · PubMed
Other PDB entries of the same protein (UniProt O75581 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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