Crystal structure of the force-sensing device region of alpha N-catenin. Determined by X-ray diffraction at 2.45 Å resolution. Released 28 Mar 2018.
Explore 5XFL in 3D Show helices and sheets RCSB PDB PDBe
5XFL contains 60 α-helices and 0 β-strands across 4 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 | 275-286 | 12 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-350 | 26 | |
| α-helix | 360-391 | 32 | |
| α-helix | 397-406 | 10 | |
| α-helix | 411-437 | 27 | |
| α-helix | 442-471 | 30 | |
| α-helix | 476-502 | 27 | |
| α-helix | 506-529 | 24 | |
| α-helix | 533-558 | 26 | |
| α-helix | 565-576 | 12 | |
| α-helix | 577-581 | 5 | |
| α-helix | 582-597 | 16 | |
| α-helix | 607-627 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 275-286 | 12 | |
| α-helix | 291-293 | 3 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-350 | 26 | |
| α-helix | 358-359 | 2 | |
| α-helix | 360-391 | 32 | |
| α-helix | 397-407 | 11 | |
| α-helix | 411-437 | 27 | |
| α-helix | 442-471 | 30 | |
| α-helix | 476-502 | 27 | |
| α-helix | 506-529 | 24 | |
| α-helix | 533-558 | 26 | |
| α-helix | 565-576 | 12 | |
| α-helix | 577-581 | 5 | |
| α-helix | 582-597 | 16 | |
| α-helix | 607-628 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 275-286 | 12 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-351 | 27 | |
| α-helix | 361-391 | 31 | |
| α-helix | 397-407 | 11 | |
| α-helix | 411-437 | 27 | |
| α-helix | 442-471 | 30 | |
| α-helix | 476-501 | 26 | |
| α-helix | 506-530 | 25 | |
| α-helix | 533-557 | 25 | |
| α-helix | 558-560 | 3 | |
| α-helix | 565-576 | 12 | |
| α-helix | 577-581 | 5 | |
| α-helix | 582-597 | 16 | |
| α-helix | 601-603 | 3 | |
| α-helix | 606-627 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 275-285 | 11 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-350 | 26 | |
| α-helix | 362-391 | 30 | |
| α-helix | 397-406 | 10 | |
| α-helix | 411-437 | 27 | |
| α-helix | 442-470 | 29 | |
| α-helix | 476-502 | 27 | |
| α-helix | 506-529 | 24 | |
| α-helix | 533-558 | 26 | |
| α-helix | 565-576 | 12 | |
| α-helix | 577-581 | 5 | |
| α-helix | 582-597 | 16 | |
| α-helix | 606-628 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Catenin alpha-2 | A, B, C, D | protein | 375 | Mus musculus | Q61301 (AlphaFold model) |
>5XFL_1 Catenin alpha-2 (chains A, B, C, D) GPATSPTDEAKGHTGIGELAAALNEFDNKIILDPMTFSEARFRPSLEERLESIISGAALM ADSSCTRDDRRERIVAECNAVRQALQDLLSEYMNNTGRKEKGDPLNIAIDKMTKKTRDLR RQLRKAVMDHISDSFLETNVPLLVLIEAAKSGNEKEVKEYAQVFREHANKLVEVANLACS ISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLT EAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAE MENYEAGVYTEKVLEATKLLSETVMPRFAEQVEVAIEALSANVPQPFEENEFIDASRLVY DGVRDIRKAVLMIRT
The force-sensing device region of alpha-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form. Hirano, Y., Amano, Y., Yonemura, S. et al. Genes Cells (2018) 23:370-385. DOI 10.1111/gtc.12578 · PubMed
Other PDB entries of the same protein (UniProt Q61301 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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