Crystal structure of JNK1 bound to a MKK7 docking motif. Determined by X-ray diffraction at 2.34 Å resolution. Released 25 Mar 2015.
Explore 4UX9 in 3D Show helices and sheets RCSB PDB PDBe
4UX9 contains 100 α-helices and 56 β-strands across 5 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 | 10-15 | 6 | 1 |
| β-strand | 18-23 | 6 | 1 |
| β-strand | 26-33 | 8 | 2 |
| β-strand | 39-45 | 7 | 2 |
| β-strand | 50-57 | 8 | 2 |
| α-helix | 64-79 | 16 | |
| β-strand | 85 | 1 | 3 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-92 | 5 | 2 |
| β-strand | 104-109 | 6 | 2 |
| α-helix | 110-111 | 2 | |
| β-strand | 113-114 | 2 | 3 |
| α-helix | 116-119 | 4 | |
| α-helix | 125-144 | 20 | |
| β-strand | 148 | 1 | 4 |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 3 |
| β-strand | 165-167 | 3 | 3 |
| β-strand | 174 | 1 | 4 |
| β-strand | 177 | 1 | 5 |
| α-helix | 189-191 | 3 | |
| α-helix | 194-197 | 4 | |
| β-strand | 202 | 1 | 5 |
| α-helix | 206-220 | 15 | |
| α-helix | 232-241 | 10 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-249 | 4 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-265 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 277-279 | 3 | |
| α-helix | 281-282 | 2 | |
| α-helix | 291-301 | 11 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 322-324 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 332-335 | 4 | |
| α-helix | 349-362 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 6 |
| β-strand | 18-23 | 6 | 6 |
| β-strand | 26-33 | 8 | 7 |
| β-strand | 40-45 | 6 | 7 |
| β-strand | 50-58 | 9 | 7 |
| α-helix | 60-62 | 3 | |
| α-helix | 64-79 | 16 | |
| β-strand | 85 | 1 | 8 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-92 | 5 | 7 |
| β-strand | 103-109 | 7 | 7 |
| β-strand | 113-114 | 2 | 8 |
| α-helix | 115-119 | 5 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-143 | 19 | |
| β-strand | 148 | 1 | 9 |
| α-helix | 154-156 | 3 | |
| β-strand | 157-160 | 4 | 8 |
| β-strand | 164-167 | 4 | 8 |
| β-strand | 174 | 1 | 9 |
| α-helix | 189-191 | 3 | |
| α-helix | 194-197 | 4 | |
| α-helix | 206-220 | 15 | |
| α-helix | 232-241 | 10 | |
| α-helix | 244-245 | 2 | |
| α-helix | 246-250 | 5 | |
| α-helix | 254-261 | 8 | |
| α-helix | 264-265 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 277-279 | 3 | |
| α-helix | 281-283 | 3 | |
| α-helix | 291-301 | 11 | |
| 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 | 332-336 | 5 | |
| α-helix | 354-361 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 10 |
| β-strand | 18-23 | 6 | 10 |
| β-strand | 26-34 | 9 | 11 |
| β-strand | 39-45 | 7 | 11 |
| β-strand | 50-58 | 9 | 11 |
| α-helix | 64-79 | 16 | |
| β-strand | 85 | 1 | 12 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-92 | 5 | 11 |
| β-strand | 103-109 | 7 | 11 |
| α-helix | 110-111 | 2 | |
| β-strand | 113-114 | 2 | 12 |
| α-helix | 115-119 | 5 | |
| α-helix | 125-144 | 20 | |
| β-strand | 148 | 1 | 13 |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 12 |
| β-strand | 165-167 | 3 | 12 |
| β-strand | 174 | 1 | 13 |
| α-helix | 189-191 | 3 | |
| α-helix | 194-197 | 4 | |
| α-helix | 206-220 | 15 | |
| α-helix | 232-241 | 10 | |
| 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 | 277-279 | 3 | |
| α-helix | 291-301 | 11 | |
| 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 | 332-336 | 5 | |
| α-helix | 349-362 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 14 |
| β-strand | 18-23 | 6 | 14 |
| β-strand | 26-31 | 6 | 15 |
| β-strand | 40-45 | 6 | 15 |
| β-strand | 50-56 | 7 | 15 |
| α-helix | 64-79 | 16 | |
| β-strand | 85 | 1 | 16 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-92 | 5 | 15 |
| β-strand | 105-109 | 5 | 15 |
| α-helix | 110-111 | 2 | |
| β-strand | 113-114 | 2 | 16 |
| α-helix | 115-119 | 5 | |
| α-helix | 122-124 | 3 | |
| α-helix | 125-143 | 19 | |
| β-strand | 148 | 1 | 17 |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 16 |
| β-strand | 165-167 | 3 | 16 |
| β-strand | 174 | 1 | 17 |
| β-strand | 177 | 1 | 18 |
| α-helix | 194-197 | 4 | |
| β-strand | 202 | 1 | 18 |
| α-helix | 206-220 | 15 | |
| α-helix | 232-241 | 10 | |
| 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 | 277-279 | 3 | |
| α-helix | 281-282 | 2 | |
| α-helix | 291-301 | 11 | |
| α-helix | 306-308 | 3 | |
| α-helix | 310-311 | 2 | |
| α-helix | 312-317 | 6 | |
| α-helix | 322-324 | 3 | |
| α-helix | 327-330 | 4 | |
| α-helix | 332-335 | 4 | |
| α-helix | 349-363 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 38-40 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 8 | A, B, C, D | protein | 364 | HOMO SAPIENS | P45983 (AlphaFold model) |
| Dual specificity mitogen-activated protein kinase kinase 7 | F, G, H, I | protein | 12 | HOMO SAPIENS | O14733 (AlphaFold model) |
>4UX9_1 MITOGEN-ACTIVATED PROTEIN KINASE 8 (chains A, B, C, D) MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRP FQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQ MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF MMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQ LGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSK MLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEV MDLE
>4UX9_2 DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 7 (chains F, G, H, I) QRPRPTLQLPLA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 4 |
Water and common crystallization additives (SO4) are not listed.
Structure and Dynamics of the Mkk7-Jnk Signaling Complex. Kragelj, J., Palencia, A., Nanao, M.H. et al. Proc Natl Acad Sci U S A (2015) 112:3409. DOI 10.1073/PNAS.1419528112 · 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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