Crystal structure of human Smad2-Ski complex. Determined by X-ray diffraction at 1.85 Å resolution. Released 28 Mar 2018.
Explore 5XOD in 3D Show helices and sheets RCSB PDB PDBe
5XOD contains 11 α-helices and 12 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 | 264-266 | 3 | |
| β-strand | 275-281 | 7 | 1 |
| β-strand | 284-285 | 2 | 1 |
| α-helix | 288-289 | 2 | |
| β-strand | 290-292 | 3 | 1 |
| β-strand | 296-300 | 5 | 2 |
| β-strand | 310-312 | 3 | 2 |
| α-helix | 323-329 | 7 | |
| β-strand | 336-341 | 6 | 2 |
| β-strand | 344-349 | 6 | 2 |
| β-strand | 355-358 | 4 | 1 |
| α-helix | 360-364 | 5 | |
| β-strand | 373-376 | 4 | 1 |
| β-strand | 381-386 | 6 | 2 |
| α-helix | 387-397 | 11 | |
| α-helix | 398-400 | 3 | |
| α-helix | 402-406 | 5 | |
| α-helix | 407-412 | 6 | |
| β-strand | 413-418 | 6 | 1 |
| α-helix | 431-433 | 3 | |
| β-strand | 437-442 | 6 | 1 |
| α-helix | 443-453 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-27 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mothers against decapentaplegic homolog 2 | A | protein | 199 | Homo sapiens | Q15796 (AlphaFold model) |
| Ski oncogene | B | protein | 31 | Homo sapiens | P12755 (AlphaFold model) |
>5XOD_1 Mothers against decapentaplegic homolog 2 (chains A) GPDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNV NRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPG CNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIE LHLNGPLQWLDKVLTQMGS
>5XOD_2 Ski oncogene (chains B) GPGLQKTLEQFHLSSMSSLGGPAAFSASDED
Hydrophobic patches on SMAD2 and SMAD3 determine selective binding to cofactors. Miyazono, K.I., Moriwaki, S., Ito, T. et al. Sci Signal (2018) 11. DOI 10.1126/scisignal.aao7227 · PubMed
Other PDB entries of the same protein (UniProt Q15796 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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