MEK1 in complex with compound 6. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Mar 2021.
Explore 7B94 in 3D Show helices and sheets RCSB PDB PDBe
7B94 contains 35 α-helices and 20 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 44-57 | 14 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 1 |
| β-strand | 80-87 | 8 | 1 |
| β-strand | 92-100 | 9 | 1 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| β-strand | 126 | 1 | 2 |
| β-strand | 129-135 | 7 | 1 |
| β-strand | 138-143 | 6 | 1 |
| β-strand | 150 | 1 | 2 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-184 | 22 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 2 |
| β-strand | 204-206 | 3 | 2 |
| α-helix | 213-218 | 6 | |
| 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 | |
| β-strand | 327 | 1 | 3 |
| β-strand | 330 | 1 | 3 |
| α-helix | 332-341 | 10 | |
| α-helix | 352-356 | 5 | |
| α-helix | 359-366 | 8 | |
| α-helix | 371-379 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-58 | 15 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 4 |
| β-strand | 80-87 | 8 | 4 |
| β-strand | 93-100 | 8 | 4 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| β-strand | 126 | 1 | 5 |
| β-strand | 129-135 | 7 | 4 |
| β-strand | 138-144 | 7 | 4 |
| β-strand | 150 | 1 | 5 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-184 | 22 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 5 |
| β-strand | 204-206 | 3 | 5 |
| α-helix | 213-218 | 6 | |
| α-helix | 232-235 | 4 | |
| α-helix | 238-240 | 3 | |
| 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 | 352-356 | 5 | |
| α-helix | 359-366 | 8 | |
| α-helix | 371-379 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dual specificity mitogen-activated protein kinase kinase 1,Dual specificity mitogen-activated… | A, B | protein | 326 | Homo sapiens | Q02750 (AlphaFold model) |
>7B94_1 Dual specificity mitogen-activated protein kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 1 (chains A, B) MAHHHHHHAAAENLYFQLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNG GVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEI SICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVN SRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVG RYPIGSGSGSMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMV HAFIKRSDAEEVDFAGWLCSTIGLNQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| T3W | 2-(4-iodophenyl)-8~{H}-imidazo[1,2-c]pyrimidin-5-one | C12 H8 I N3 O | 2 |
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Water and common crystallization additives (SO4) are not listed.
Fragment-Based Discovery of Novel Allosteric MEK1 Binders. Di Fruscia, P., Edfeldt, F., Shamovsky, I. et al. ACS Med Chem Lett (2021) 12:302-308. DOI 10.1021/acsmedchemlett.0c00563 · 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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