Structure of Human Mad1 C-terminal Domain Reveals Its Involvement in Kinetochore Targeting. Determined by X-ray diffraction at 1.76 Å resolution. Released 11 Apr 2012.
Explore 4DZO in 3D Show helices and sheets RCSB PDB PDBe
4DZO contains 12 α-helices and 8 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 | 599-637 | 39 | |
| β-strand | 639-644 | 6 | 1 |
| β-strand | 648-653 | 6 | 1 |
| β-strand | 663-667 | 5 | 1 |
| β-strand | 675-678 | 4 | 1 |
| α-helix | 679 | 1 | |
| α-helix | 683-685 | 3 | |
| α-helix | 687-689 | 3 | |
| α-helix | 690-695 | 6 | |
| α-helix | 700-715 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 599-637 | 39 | |
| β-strand | 639-643 | 5 | 2 |
| β-strand | 649-653 | 5 | 2 |
| β-strand | 663-667 | 5 | 2 |
| β-strand | 675-678 | 4 | 2 |
| α-helix | 679 | 1 | |
| α-helix | 681-684 | 4 | |
| α-helix | 687-689 | 3 | |
| α-helix | 690-696 | 7 | |
| α-helix | 700-715 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitotic spindle assembly checkpoint protein MAD1 | A, B | protein | 123 | Homo sapiens | Q9Y6D9 (AlphaFold model) |
>4DZO_1 Mitotic spindle assembly checkpoint protein MAD1 (chains A, B) GSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLY AEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQ TVA
Structure of human Mad1 C-terminal domain reveals its involvement in kinetochore targeting. Kim, S., Sun, H., Tomchick, D.R. et al. Proc Natl Acad Sci U S A (2012) 109:6549-6554. DOI 10.1073/pnas.1118210109 · PubMed
Other PDB entries of the same protein (UniProt Q9Y6D9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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