Solution structure of the spindle assembly checkpoint protein human MAD2. Determined by solution NMR. Released 8 Mar 2000.
Explore 1DUJ in 3D Show helices and sheets RCSB PDB PDBe
1DUJ contains 4 α-helices and 10 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 12-14 | 3 | 1 |
| β-strand | 17 | 1 | 2 |
| α-helix | 19-32 | 14 | |
| α-helix | 33-37 | 5 | |
| β-strand | 46-50 | 5 | 3 |
| β-strand | 53-57 | 5 | 3 |
| α-helix | 61-75 | 15 | |
| β-strand | 85-92 | 8 | 1 |
| β-strand | 97-105 | 9 | 1 |
| β-strand | 108 | 1 | 2 |
| α-helix | 124-143 | 20 | |
| β-strand | 151-160 | 10 | 1 |
| β-strand | 175-177 | 3 | 1 |
| β-strand | 187-195 | 9 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spindle assembly checkpoint protein | A | protein | 187 | Homo sapiens | Q13257 (AlphaFold model) |
>1DUJ_1 SPINDLE ASSEMBLY CHECKPOINT PROTEIN (chains A) GSITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNV VEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEI RSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTT TIHKVNS
Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20. Luo, X., Fang, G., Coldiron, M. et al. Nat Struct Biol (2000) 7:224-229. DOI 10.1038/73338 · PubMed
Other PDB entries of the same protein (UniProt Q13257 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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