Cryo-EM structure of ARAF-MEK1 complex with GDC-0879 and a covalent MEK inhibitor TWG-07-148. Determined by electron microscopy at 2.51 Å resolution. Released 16 Sept 2026.
Explore 9ZDQ in 3D Show helices and sheets RCSB PDB PDBe
9ZDQ contains 58 α-helices and 46 β-strands across 4 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 | 304 | 1 | 1 |
| β-strand | 311-318 | 8 | 1 |
| β-strand | 322-328 | 7 | 1 |
| β-strand | 332-338 | 7 | 1 |
| α-helix | 345-359 | 15 | |
| β-strand | 366 | 1 | 2 |
| β-strand | 369-373 | 5 | 1 |
| β-strand | 379-383 | 5 | 1 |
| β-strand | 389 | 1 | 2 |
| α-helix | 390-391 | 2 | |
| α-helix | 392-397 | 6 | |
| α-helix | 403-422 | 20 | |
| β-strand | 425-426 | 2 | 3 |
| α-helix | 432-434 | 3 | |
| β-strand | 435-438 | 4 | 2 |
| β-strand | 442-445 | 4 | 2 |
| β-strand | 452-453 | 2 | 3 |
| β-strand | 469 | 1 | 4 |
| α-helix | 470-472 | 3 | |
| α-helix | 475-479 | 5 | |
| α-helix | 488-504 | 17 | |
| α-helix | 515-523 | 9 | |
| α-helix | 531-533 | 3 | |
| α-helix | 540-549 | 10 | |
| α-helix | 554-556 | 3 | |
| α-helix | 558-559 | 2 | |
| α-helix | 560-571 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 68-76 | 9 | 5 |
| β-strand | 81-87 | 7 | 5 |
| β-strand | 92-100 | 9 | 5 |
| α-helix | 105-114 | 10 | |
| α-helix | 115-120 | 6 | |
| β-strand | 126 | 1 | 6 |
| β-strand | 129-134 | 6 | 5 |
| β-strand | 138-144 | 7 | 5 |
| β-strand | 150 | 1 | 6 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-182 | 20 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 6 |
| β-strand | 204-206 | 3 | 6 |
| α-helix | 213-218 | 6 | |
| β-strand | 223 | 1 | 4 |
| α-helix | 232-236 | 5 | |
| α-helix | 242-258 | 17 | |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 325-326 | 2 | |
| α-helix | 332-341 | 10 | |
| α-helix | 352-355 | 4 | |
| α-helix | 359-366 | 8 | |
| α-helix | 371-379 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase A-Raf | A, C | protein | 273 | Homo sapiens | P10398 (AlphaFold model) |
| Dual specificity mitogen-activated protein kinase kinase 1 | B, D | protein | 317 | Homo sapiens | Q02750 (AlphaFold model) |
>9ZDQ_1 Serine/threonine-protein kinase A-Raf (chains A, C) DWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKT RHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLH AKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQ DPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKA MRRLLSDCLKFQREERPLFPQILATIELLQRSL
>9ZDQ_2 Dual specificity mitogen-activated protein kinase kinase 1 (chains B, D) DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPY IVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHK IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDAMANAFVGTRSYMSPERLQGTHYSVQSD IWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR PPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSD AEEVDFAGWLCSTIGLN
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1C1Y | N-{(3M)-3-[3-cyclopropyl-5-(2-fluoro-4-iodoanilino)-6,8-dimethyl-2,4,7-trioxo-3… | C27 H25 F I N5 O4 | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
| 29L | 2-{4-[(1E)-1-(hydroxyimino)-2,3-dihydro-1H-inden-5-yl]-3-(pyridin-4-yl)-1H-pyra… | C19 H18 N4 O2 | 2 |
cryo-EM structure of ARAF-MEK1 complex with GDC-0879 and a covalent MEK inhibitor TWG-07-148. Chakraborty, S., Eck, M.J. To be published.
Other PDB entries of the same protein (UniProt P10398 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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