Crystal structure of budding yeast Cdc5 polo-box domain in complex with Spc72 phosphopeptide. Determined by X-ray diffraction at 2.7 Å resolution. Released 19 Feb 2020.
Explore 6MF5 in 3D Show helices and sheets RCSB PDB PDBe
6MF5 contains 16 α-helices and 32 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 | 437-450 | 14 | |
| β-strand | 464-465 | 2 | 1 |
| α-helix | 471-492 | 22 | |
| α-helix | 510-512 | 3 | |
| β-strand | 514-520 | 7 | 2 |
| β-strand | 525-530 | 6 | 2 |
| β-strand | 535-538 | 4 | 2 |
| β-strand | 544-547 | 4 | 2 |
| β-strand | 553-560 | 8 | 2 |
| β-strand | 564-571 | 8 | 2 |
| α-helix | 580-596 | 17 | |
| β-strand | 597 | 1 | 3 |
| β-strand | 615-620 | 6 | 1 |
| β-strand | 624-629 | 6 | 1 |
| β-strand | 634-638 | 5 | 1 |
| β-strand | 643-647 | 5 | 1 |
| α-helix | 648-650 | 3 | |
| β-strand | 652-656 | 5 | 1 |
| β-strand | 662-666 | 5 | 1 |
| α-helix | 667-673 | 7 | |
| α-helix | 684-698 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 437-451 | 15 | |
| β-strand | 464-465 | 2 | 4 |
| α-helix | 466-468 | 3 | |
| α-helix | 471-496 | 26 | |
| α-helix | 510-512 | 3 | |
| β-strand | 514-519 | 6 | 5 |
| α-helix | 521-524 | 4 | |
| β-strand | 526-530 | 5 | 5 |
| β-strand | 535-538 | 4 | 5 |
| β-strand | 544-547 | 4 | 5 |
| β-strand | 553-559 | 7 | 5 |
| β-strand | 565-571 | 7 | 5 |
| α-helix | 582-596 | 15 | |
| β-strand | 597 | 1 | 6 |
| α-helix | 598-600 | 3 | |
| β-strand | 615-620 | 6 | 4 |
| β-strand | 624-629 | 6 | 4 |
| β-strand | 634-638 | 5 | 4 |
| β-strand | 643-647 | 5 | 4 |
| β-strand | 652-656 | 5 | 4 |
| β-strand | 662-666 | 5 | 4 |
| α-helix | 667-673 | 7 | |
| α-helix | 684-700 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 229-230 | 2 | 2 |
| β-strand | 233 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell cycle serine/threonine-protein kinase CDC5/MSD2 | A, B | protein | 290 | Saccharomyces cerevisiae | P32562 (AlphaFold model) |
| Spc72 | C, D | protein | 11 | Saccharomyces cerevisiae | P39723 (AlphaFold model) |
>6MF5_1 Cell cycle serine/threonine-protein kinase CDC5/MSD2 (chains A, B) GALSPGGTKQKYKEVVDIEAQRRLNDLAREARIRRAQQAVLRKELIATSTNVIKSEISLR ILASECHLTLNGIVEAEAQYKMGGLPKSRLPKIKHPMIVTKWVDYSNKHGFSYQLSTEDI GVLFNNGTTVLRLADAEEFWYISYDDREGWVASHYLLSEKPRELSRHLEVVDFFAKYMKA NLSRVSTFGREEYHKDDVFLRRYTRYKPFVMFELSDGTFQFNFKDHHKMAISDGGKLVTY ISPSHESTTYPLVEVLKYGEIPGYPESNFREKLTLIKEGLKQKSTIVTVD
>6MF5_2 Spc72 (chains C, D) SLAQSSPAGSQ
Distinct surfaces on Cdc5/PLK Polo-box domain orchestrate combinatorial substrate recognition during cell division. Almawi, A.W., Langlois-Lemay, L., Boulton, S. et al. Sci Rep (2020) 10:3379-3379. DOI 10.1038/s41598-020-60344-4 · PubMed
Other PDB entries of the same protein (UniProt P32562 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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