Crystal structure of p120 catenin in complex with E-cadherin. Determined by X-ray diffraction at 3.0 Å resolution. Released 21 Apr 2010.
Explore 3L6Y in 3D Show helices and sheets RCSB PDB PDBe
3L6Y contains 84 α-helices and 0 β-strands across 6 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 |
|---|---|---|---|
| α-helix | 368-374 | 7 | |
| α-helix | 380-394 | 15 | |
| α-helix | 398-406 | 9 | |
| α-helix | 409-416 | 8 | |
| α-helix | 422-435 | 14 | |
| α-helix | 441-449 | 9 | |
| α-helix | 452-462 | 11 | |
| α-helix | 466-480 | 15 | |
| α-helix | 483-496 | 14 | |
| α-helix | 497-502 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 524-537 | 14 | |
| α-helix | 542-549 | 8 | |
| α-helix | 554-566 | 13 | |
| α-helix | 574-587 | 14 | |
| α-helix | 590-593 | 4 | |
| α-helix | 649-654 | 6 | |
| α-helix | 656-668 | 13 | |
| α-helix | 672-687 | 16 | |
| α-helix | 691-700 | 10 | |
| α-helix | 703-711 | 9 | |
| α-helix | 712-714 | 3 | |
| α-helix | 718-732 | 15 | |
| α-helix | 738-745 | 8 | |
| α-helix | 766-779 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 771-773 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 364-367 | 4 | |
| α-helix | 368-374 | 7 | |
| α-helix | 380-394 | 15 | |
| α-helix | 398-406 | 9 | |
| α-helix | 409-416 | 8 | |
| α-helix | 422-435 | 14 | |
| α-helix | 441-449 | 9 | |
| α-helix | 452-462 | 11 | |
| α-helix | 466-480 | 15 | |
| α-helix | 483-496 | 14 | |
| α-helix | 497-502 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 524-537 | 14 | |
| α-helix | 542-549 | 8 | |
| α-helix | 554-566 | 13 | |
| α-helix | 574-587 | 14 | |
| α-helix | 590-593 | 4 | |
| α-helix | 649-654 | 6 | |
| α-helix | 656-668 | 13 | |
| α-helix | 672-687 | 16 | |
| α-helix | 691-700 | 10 | |
| α-helix | 703-711 | 9 | |
| α-helix | 712-714 | 3 | |
| α-helix | 718-732 | 15 | |
| α-helix | 738-750 | 13 | |
| α-helix | 766-779 | 14 | |
| α-helix | 810-822 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 364-367 | 4 | |
| α-helix | 368-374 | 7 | |
| α-helix | 380-394 | 15 | |
| α-helix | 398-406 | 9 | |
| α-helix | 409-416 | 8 | |
| α-helix | 422-435 | 14 | |
| α-helix | 441-449 | 9 | |
| α-helix | 452-462 | 11 | |
| α-helix | 466-480 | 15 | |
| α-helix | 483-496 | 14 | |
| α-helix | 497-502 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 524-537 | 14 | |
| α-helix | 542-549 | 8 | |
| α-helix | 554-566 | 13 | |
| α-helix | 574-587 | 14 | |
| α-helix | 590-593 | 4 | |
| α-helix | 649-654 | 6 | |
| α-helix | 656-668 | 13 | |
| α-helix | 672-687 | 16 | |
| α-helix | 691-700 | 10 | |
| α-helix | 703-711 | 9 | |
| α-helix | 712-714 | 3 | |
| α-helix | 718-731 | 14 | |
| α-helix | 732-734 | 3 | |
| α-helix | 738-752 | 15 | |
| α-helix | 766-779 | 14 | |
| α-helix | 796-803 | 8 | |
| α-helix | 810-823 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Catenin delta-1 | A, C, E | protein | 584 | Homo sapiens | O60716 (AlphaFold model) |
| E-cadherin | B, D, F | protein | 18 | P12830 (AlphaFold model) |
>3L6Y_1 Catenin delta-1 (chains A, C, E) GSPEFMIGEEVPSDQYYWAPLAQHERGSLASLDSLRKGGPPPPNWRQPELPEVIAMLGFR LDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPVLVGLLDHPKKEVHLGACGALKNISFG RDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALT DEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDAL IFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEAAPNVANNTGTSPARG YELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAI ADLLTNEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTV ISILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKEL RKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIQMSNMGS NTKSLDNNYSTPNERGDHNRTLDRSGDLGDMEPLKGTTPLMQKI
>3L6Y_2 E-cadherin (chains B, D, F) DEEGGGEEDQDFDLSQLH
Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion. Ishiyama, N., Lee, S.H., Liu, S. et al. Cell (2010) 141:117-128. DOI 10.1016/j.cell.2010.01.017 · PubMed
Other PDB entries of the same protein (UniProt O60716 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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