Crystal structure of MEK1 C121S mutant. Determined by X-ray diffraction at 2.01 Å resolution. Released 22 Jun 2022.
Explore 7F2X in 3D Show helices and sheets RCSB PDB PDBe
7F2X contains 16 α-helices and 9 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 | 44-60 | 17 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-77 | 10 | 1 |
| β-strand | 80-87 | 8 | 1 |
| β-strand | 92-100 | 9 | 1 |
| α-helix | 105-118 | 14 | |
| β-strand | 126 | 1 | 2 |
| β-strand | 129-134 | 6 | 1 |
| β-strand | 138-144 | 7 | 1 |
| β-strand | 149-150 | 2 | 2 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-183 | 21 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 2 |
| β-strand | 204-206 | 3 | 2 |
| α-helix | 213-221 | 9 | |
| α-helix | 232-238 | 7 | |
| α-helix | 242-258 | 17 | |
| α-helix | 269-281 | 13 | |
| α-helix | 283-285 | 3 | |
| α-helix | 287-288 | 2 | |
| α-helix | 294-303 | 10 | |
| α-helix | 314-318 | 5 | |
| α-helix | 321-328 | 8 | |
| α-helix | 333-340 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MEK1 F11 | A | protein | 321 | Homo sapiens | Q02750 (AlphaFold model) |
>7F2X_1 MEK1 F11 (chains A) MTLQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHL EIKPAIRNQIIRELQVLHESNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRI PEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMAN SFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIGSGSGSMAIFELLDYIVN EPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTI GLNQPSTPTHAAGEGHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Qualitative differences in disease-associated MEK mutants reveal molecular signatures and aberrant signaling-crosstalk in cancer. Kubota, Y., Fujioka, Y., Patil, A. et al. Nat Commun (2022) 13:4063-4063. DOI 10.1038/s41467-022-31690-w · PubMed
Other PDB entries of the same protein (UniProt Q02750 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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