Optimization of Microtubule Affinity Regulating Kinase (MARK) Inhibitors with Improved Physical Properties. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Feb 2016.
Explore 5EAK in 3D Show helices and sheets RCSB PDB PDBe
5EAK contains 40 α-helices and 19 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 |
|---|---|---|---|
| β-strand | 50 | 1 | 1 |
| β-strand | 53-61 | 9 | 1 |
| β-strand | 65-72 | 8 | 1 |
| β-strand | 78-85 | 8 | 1 |
| α-helix | 86-88 | 3 | |
| α-helix | 91-106 | 16 | |
| β-strand | 112 | 1 | 2 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-120 | 6 | 1 |
| β-strand | 124-130 | 7 | 1 |
| β-strand | 135-136 | 2 | 2 |
| α-helix | 137-144 | 8 | |
| α-helix | 149-168 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 181-183 | 3 | 2 |
| β-strand | 189-191 | 3 | 2 |
| α-helix | 213-215 | 3 | |
| α-helix | 218-222 | 5 | |
| α-helix | 229-245 | 17 | |
| α-helix | 255-264 | 10 | |
| α-helix | 267-270 | 4 | |
| α-helix | 275-284 | 10 | |
| α-helix | 289-291 | 3 | |
| α-helix | 293-294 | 2 | |
| α-helix | 295-298 | 4 | |
| α-helix | 302-305 | 4 | |
| α-helix | 318-321 | 4 | |
| α-helix | 326-333 | 8 | |
| α-helix | 339-347 | 9 | |
| α-helix | 353-360 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 53-61 | 9 | 3 |
| β-strand | 65-72 | 8 | 3 |
| β-strand | 78-85 | 8 | 3 |
| α-helix | 86-88 | 3 | |
| α-helix | 91-106 | 16 | |
| β-strand | 112 | 1 | 4 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-120 | 6 | 3 |
| β-strand | 124-129 | 6 | 3 |
| β-strand | 135-136 | 2 | 4 |
| α-helix | 137-144 | 8 | |
| α-helix | 149-168 | 20 | |
| α-helix | 178-180 | 3 | |
| β-strand | 181-183 | 3 | 4 |
| β-strand | 189-191 | 3 | 4 |
| α-helix | 213-215 | 3 | |
| α-helix | 218-222 | 5 | |
| α-helix | 229-245 | 17 | |
| α-helix | 255-264 | 10 | |
| α-helix | 268-270 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 289-291 | 3 | |
| α-helix | 293-294 | 2 | |
| α-helix | 295-298 | 4 | |
| α-helix | 302-305 | 4 | |
| α-helix | 318-321 | 4 | |
| α-helix | 326-333 | 8 | |
| α-helix | 339-347 | 9 | |
| α-helix | 353-360 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase MARK2 | A, B | protein | 328 | Homo sapiens | Q7KZI7 (AlphaFold model) |
>5EAK_1 Serine/threonine-protein kinase MARK2 (chains A, B) KLNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQK LFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKF RQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYA APELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTD CENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMG YTREEIQDSLVGQRYNEVMATYLLLGYK
| ID | Name | Formula | Copies |
|---|---|---|---|
| 24R | N-[(1S,2R)-2-aminocyclohexyl]-4-[6-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyr… | C21 H23 N7 O S | 2 |
Optimization of microtubule affinity regulating kinase (MARK) inhibitors with improved physical properties. Sloman, D.L., Noucti, N., Altman, M.D. et al. Bioorg Med Chem Lett (2016) 26:4362-4366. DOI 10.1016/j.bmcl.2016.02.003 · PubMed
Other PDB entries of the same protein (UniProt Q7KZI7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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