JNK1 covalently bound to BD837 cyclohexenone based inhibitor. Determined by X-ray diffraction at 2.41 Å resolution. Released 24 Jul 2024.
Explore 8PTA in 3D Show helices and sheets RCSB PDB PDBe
8PTA contains 62 α-helices and 34 β-strands across 3 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 | 10-13 | 4 | 1 |
| β-strand | 20-23 | 4 | 1 |
| β-strand | 26-31 | 6 | 2 |
| β-strand | 40-45 | 6 | 2 |
| β-strand | 51-57 | 7 | 2 |
| α-helix | 64-78 | 15 | |
| β-strand | 85 | 1 | 3 |
| β-strand | 88-92 | 5 | 2 |
| β-strand | 104-109 | 6 | 2 |
| β-strand | 113-114 | 2 | 3 |
| α-helix | 115-120 | 6 | |
| α-helix | 125-144 | 20 | |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 3 |
| β-strand | 165-167 | 3 | 3 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-220 | 15 | |
| α-helix | 230-241 | 12 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-250 | 5 | |
| α-helix | 254-262 | 9 | |
| α-helix | 264-265 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 285-301 | 17 | |
| α-helix | 306-308 | 3 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-316 | 5 | |
| α-helix | 322-324 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 332-335 | 4 | |
| α-helix | 349-361 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-12 | 3 | 4 |
| β-strand | 21-23 | 3 | 4 |
| β-strand | 26-31 | 6 | 5 |
| β-strand | 39-45 | 7 | 5 |
| β-strand | 50-58 | 9 | 5 |
| α-helix | 60-62 | 3 | |
| α-helix | 64-79 | 16 | |
| β-strand | 82 | 1 | 6 |
| β-strand | 85 | 1 | 6 |
| β-strand | 88-92 | 5 | 5 |
| α-helix | 98-100 | 3 | |
| β-strand | 103-109 | 7 | 5 |
| β-strand | 113-114 | 2 | 6 |
| α-helix | 115-120 | 6 | |
| α-helix | 125-144 | 20 | |
| β-strand | 157-159 | 3 | 6 |
| β-strand | 165-167 | 3 | 6 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-220 | 15 | |
| α-helix | 230-241 | 12 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-250 | 5 | |
| α-helix | 254-262 | 9 | |
| α-helix | 264-265 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 285-301 | 17 | |
| α-helix | 306-308 | 3 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-316 | 5 | |
| α-helix | 322-324 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 332-334 | 3 | |
| α-helix | 349-361 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 7 |
| β-strand | 18-23 | 6 | 7 |
| β-strand | 26-31 | 6 | 8 |
| β-strand | 39-45 | 7 | 8 |
| β-strand | 50-56 | 7 | 8 |
| α-helix | 57 | 1 | |
| α-helix | 64-78 | 15 | |
| β-strand | 85 | 1 | 9 |
| β-strand | 88-92 | 5 | 8 |
| β-strand | 105-109 | 5 | 8 |
| β-strand | 113-114 | 2 | 9 |
| α-helix | 115-120 | 6 | |
| α-helix | 125-144 | 20 | |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 9 |
| β-strand | 165-167 | 3 | 9 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-220 | 15 | |
| α-helix | 232-240 | 9 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-249 | 4 | |
| α-helix | 254-262 | 9 | |
| α-helix | 264-265 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 285-301 | 17 | |
| α-helix | 306-308 | 3 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-316 | 5 | |
| α-helix | 319-322 | 4 | |
| α-helix | 327-330 | 4 | |
| α-helix | 332-335 | 4 | |
| α-helix | 349-359 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 8 | A, B, C | protein | 366 | Homo sapiens | P45983 (AlphaFold model) |
>8PTA_1 Mitogen-activated protein kinase 8 (chains A, B, C) GSMSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLS RPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQV IQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGT SFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVI EQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLL SKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYK EVMDLE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CIF | methyl (1R,3S)-1-methyl-3-[[3-[[3-methyl-4-[(4-pyridin-3-ylpyrimidin-2-yl)amino… | C33 H32 N6 O5 | 3 |
Water and common crystallization additives (GOL) are not listed.
Reversible covalent c-Jun N-terminal kinase inhibitors targeting a specific cysteine by precision-guided Michael-acceptor warheads. Balint, D., Poti, A.L., Alexa, A. et al. Nat Commun (2024) 15:8606-8606. DOI 10.1038/s41467-024-52573-2 · PubMed
Other PDB entries of the same protein (UniProt P45983 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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