The crystal structure of inactive p38 complexed with a ATF2 from 46 to 90. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Mar 2025.
Explore 8YPF in 3D Show helices and sheets RCSB PDB PDBe
8YPF contains 25 α-helices and 11 β-strands across 1 chain. 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 | 6-7 | 2 | |
| β-strand | 8-13 | 6 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 24-31 | 8 | 2 |
| β-strand | 36-43 | 8 | 2 |
| β-strand | 48-55 | 8 | 2 |
| α-helix | 62-77 | 16 | |
| β-strand | 83 | 1 | 3 |
| β-strand | 88-90 | 3 | 2 |
| β-strand | 103-107 | 5 | 2 |
| β-strand | 111-112 | 2 | 3 |
| α-helix | 113-118 | 6 | |
| α-helix | 121-123 | 3 | |
| α-helix | 124-143 | 20 | |
| α-helix | 153-155 | 3 | |
| β-strand | 156-158 | 3 | 3 |
| β-strand | 164-166 | 3 | 3 |
| α-helix | 186-188 | 3 | |
| α-helix | 191-194 | 4 | |
| α-helix | 199-201 | 3 | |
| α-helix | 204-218 | 15 | |
| α-helix | 228-239 | 12 | |
| α-helix | 244-247 | 4 | |
| α-helix | 253-261 | 9 | |
| α-helix | 263-264 | 2 | |
| α-helix | 266-268 | 3 | |
| α-helix | 270-272 | 3 | |
| α-helix | 279-288 | 10 | |
| α-helix | 293-295 | 3 | |
| α-helix | 297-298 | 2 | |
| α-helix | 299-303 | 5 | |
| α-helix | 306-308 | 3 | |
| α-helix | 318-322 | 5 | |
| α-helix | 326-329 | 4 | |
| α-helix | 334-346 | 13 | |
| α-helix | 350-352 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 14 | A | protein | 360 | Mus musculus | P47811 (AlphaFold model) |
| Cyclic AMP-dependent transcription factor ATF-2 | B | protein | 45 | Homo sapiens | P15336 (AlphaFold model) |
>8YPF_1 Mitogen-activated protein kinase 14 (chains A) MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQ SIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQ KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMT GYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVG TPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAA QALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
>8YPF_2 Cyclic AMP-dependent transcription factor ATF-2 (chains B) KHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELAS
Structural and mechanistic insights into the allosteric activation of p38alpha MAP kinase via specific docking interactions. Zhang, Y.Y., Pei, C.J., He, Q.Q. et al. To be published.
Other PDB entries of the same protein (UniProt P47811 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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