Crystal structure of p120 catenin in complex with E-cadherin. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Apr 2010.
Explore 3L6X in 3D Show helices and sheets RCSB PDB PDBe
3L6X contains 35 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 368-374 | 7 | |
| α-helix | 380-394 | 15 | |
| α-helix | 398-406 | 9 | |
| α-helix | 409-415 | 7 | |
| α-helix | 416-418 | 3 | |
| α-helix | 422-435 | 14 | |
| α-helix | 441-449 | 9 | |
| α-helix | 452-462 | 11 | |
| α-helix | 466-479 | 14 | |
| α-helix | 483-485 | 3 | |
| α-helix | 486-492 | 7 | |
| α-helix | 494-496 | 3 | |
| α-helix | 497-502 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 524-537 | 14 | |
| α-helix | 542-550 | 9 | |
| α-helix | 554-567 | 14 | |
| α-helix | 574-587 | 14 | |
| α-helix | 590-593 | 4 | |
| α-helix | 649-654 | 6 | |
| α-helix | 656-668 | 13 | |
| α-helix | 672-686 | 15 | |
| α-helix | 691-700 | 10 | |
| α-helix | 703-711 | 9 | |
| α-helix | 712-714 | 3 | |
| α-helix | 718-732 | 15 | |
| α-helix | 738-751 | 14 | |
| α-helix | 760-762 | 3 | |
| α-helix | 766-780 | 15 | |
| α-helix | 784-792 | 9 | |
| α-helix | 795-803 | 9 | |
| α-helix | 810-824 | 15 | |
| α-helix | 827-834 | 8 | |
| α-helix | 840-843 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 771-773 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Catenin delta-1 | A | protein | 584 | Homo sapiens | O60716 (AlphaFold model) |
| E-cadherin | B | protein | 18 | P12830 (AlphaFold model) |
>3L6X_1 Catenin delta-1 (chains A) GSPEFMIGEEVPSDQYYWAPLAQHERGSLASLDSLRKGGPPPPNWRQPELPEVIAMLGFR LDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPVLVGLLDHPKKEVHLGACGALKNISFG RDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALT DEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDAL IFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEAAPNVANNTGTSPARG YELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAI ADLLTNEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTV ISILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKEL RKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIQMSNMGS NTKSLDNNYSTPNERGDHNRTLDRSGDLGDMEPLKGTTPLMQKI
>3L6X_2 E-cadherin (chains B) 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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