Structural and thermodynamic characterization of cadherin-beta-catenin-alpha-catenin complex formation. Determined by X-ray diffraction at 2.8 Å resolution. Released 9 Apr 2014.
Explore 4ONS in 3D Show helices and sheets RCSB PDB PDBe
4ONS contains 23 α-helices and 2 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 | 22-35 | 14 | |
| α-helix | 55-81 | 27 | |
| α-helix | 86-112 | 27 | |
| α-helix | 117-164 | 48 | |
| α-helix | 169-196 | 28 | |
| α-helix | 200-228 | 29 | |
| α-helix | 234-258 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 85-88 | 4 | |
| α-helix | 90-98 | 9 | |
| α-helix | 100-102 | 3 | |
| α-helix | 121-140 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-35 | 14 | |
| α-helix | 55-81 | 27 | |
| α-helix | 86-112 | 27 | |
| α-helix | 117-163 | 47 | |
| α-helix | 175-184 | 10 | |
| α-helix | 189-194 | 6 | |
| α-helix | 208-227 | 20 | |
| α-helix | 238-257 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 85-88 | 4 | |
| α-helix | 90-98 | 9 | |
| α-helix | 100-102 | 3 | |
| β-strand | 115 | 1 | 1 |
| β-strand | 118 | 1 | 1 |
| α-helix | 121-140 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Catenin alpha-2 | A, C | protein | 248 | Mus musculus | Q61301 (AlphaFold model) |
| Catenin beta-1 | B, D | protein | 88 | Mus musculus | Q02248 (AlphaFold model) |
>4ONS_1 Catenin alpha-2 (chains A, C) MEIRTLTVERLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGE QIAKESQDLKEELVAAVEDVRKQGETMRIASSEFADDPCSSVKRGTMVRAARALLSAVTR LLILADMADVMRLLSHLKIVEEALEAVKNATNEQDLANRFKEFGKEMVKLNYVAARRQQE LKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGISS AAQATSPT
>4ONS_2 Catenin beta-1 (chains B, D) MGSSHHHHHHSQDPQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQ RLAEPSQMLKHAVVNLINYQDDAELATR
Structural and Thermodynamic Characterization of Cadherin beta-Catenin alpha-Catenin Complex Formation. Pokutta, S., Choi, H.J., Ahlsen, G. et al. J Biol Chem (2014) 289:13589-13601. DOI 10.1074/jbc.M114.554709 · 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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