JNK3 (Mitogen-activated protein kinase 10) in Complex with Compound 23 bearing a C(sp3)F2Br moiety. Determined by X-ray diffraction at 1.86 Å resolution. Released 2 Aug 2023.
Explore 8BZP in 3D Show helices and sheets RCSB PDB PDBe
8BZP contains 42 α-helices and 22 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 | 48-53 | 6 | 1 |
| β-strand | 56-61 | 6 | 1 |
| β-strand | 64-72 | 9 | 2 |
| β-strand | 76-83 | 8 | 2 |
| β-strand | 88-95 | 8 | 2 |
| α-helix | 102-117 | 16 | |
| β-strand | 123 | 1 | 3 |
| β-strand | 126-130 | 5 | 2 |
| β-strand | 143-147 | 5 | 2 |
| α-helix | 148-149 | 2 | |
| β-strand | 151-152 | 2 | 3 |
| α-helix | 153-157 | 5 | |
| α-helix | 160-161 | 2 | |
| α-helix | 163-182 | 20 | |
| α-helix | 192-194 | 3 | |
| β-strand | 195-197 | 3 | 3 |
| β-strand | 203-205 | 3 | 3 |
| α-helix | 232-235 | 4 | |
| α-helix | 244-258 | 15 | |
| α-helix | 268-279 | 12 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-289 | 6 | |
| α-helix | 294-299 | 6 | |
| α-helix | 302-303 | 2 | |
| α-helix | 309-312 | 4 | |
| α-helix | 315-317 | 3 | |
| α-helix | 323-339 | 17 | |
| α-helix | 344-346 | 3 | |
| α-helix | 348-349 | 2 | |
| α-helix | 350-355 | 6 | |
| α-helix | 357-360 | 4 | |
| α-helix | 365-368 | 4 | |
| α-helix | 370-373 | 4 | |
| α-helix | 387-399 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 48-52 | 5 | 4 |
| β-strand | 57-61 | 5 | 4 |
| β-strand | 64-69 | 6 | 5 |
| β-strand | 77-83 | 7 | 5 |
| β-strand | 88-96 | 9 | 5 |
| α-helix | 102-117 | 16 | |
| β-strand | 123 | 1 | 6 |
| β-strand | 126-130 | 5 | 5 |
| β-strand | 141-147 | 7 | 5 |
| β-strand | 151-152 | 2 | 6 |
| α-helix | 153-158 | 6 | |
| α-helix | 163-182 | 20 | |
| α-helix | 192-194 | 3 | |
| β-strand | 195-197 | 3 | 6 |
| β-strand | 203-205 | 3 | 6 |
| α-helix | 232-235 | 4 | |
| α-helix | 244-258 | 15 | |
| α-helix | 268-279 | 12 | |
| α-helix | 281-283 | 3 | |
| α-helix | 284-288 | 5 | |
| α-helix | 292-300 | 9 | |
| α-helix | 309-312 | 4 | |
| α-helix | 315-317 | 3 | |
| α-helix | 323-339 | 17 | |
| α-helix | 348-349 | 2 | |
| α-helix | 350-354 | 5 | |
| α-helix | 360-362 | 3 | |
| α-helix | 365-368 | 4 | |
| α-helix | 370-373 | 4 | |
| α-helix | 387-399 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 10 | A, B | protein | 364 | Homo sapiens | P53779 (AlphaFold model) |
>8BZP_1 Mitogen-activated protein kinase 10 (chains A, B) MSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRP FQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQ MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQ LGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSK MLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEV MNSE
| ID | Name | Formula | Copies |
|---|---|---|---|
| SWM | 2-bromanyl-2,2-bis(fluoranyl)-~{N}-(5-pyridin-4-yl-1,3,4-thiadiazol-2-yl)ethana… | C9 H5 Br F2 N4 O S | 2 |
| C15 | N-dodecyl-n,n-dimethyl-3-ammonio-1-propanesulfonate | C17 H38 N O3 S | 3 |
Water and common crystallization additives (EDO, GOL, BME, PEG, CL) are not listed.
Principles and Applications of CF 2 X Moieties as Unconventional Halogen Bond Donors in Medicinal Chemistry, Chemical Biology, and Drug Discovery. Vaas, S., Zimmermann, M.O., Schollmeyer, D. et al. J Med Chem (2023) 66:10202-10225. DOI 10.1021/acs.jmedchem.3c00634 · PubMed
Other PDB entries of the same protein (UniProt P53779 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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