4MNE: BRAF:MEK1 complex
Crystal structure of the BRAF:MEK1 complex. Determined by X-ray diffraction at 2.85 Å resolution. Released 18 Jun 2014.
- Method
- X-ray diffraction
- Resolution
- 2.85 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 17,682
- Mol. weight
- 297.71 kDa
- Ligands
- MG, 573, ACP
- Released
- 18 Jun 2014
Explore 4MNE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4MNE contains 126 α-helices and 95 β-strands across 8 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.
Chain A: 19 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 1 |
| β-strand | 80-87 | 8 | 1 |
| β-strand | 93-100 | 8 | 1 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| β-strand | 123 | 1 | 2 |
| β-strand | 126 | 1 | 2 |
| β-strand | 129-135 | 7 | 1 |
| β-strand | 138-144 | 7 | 1 |
| β-strand | 149-150 | 2 | 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 | |
| β-strand | 223 | 1 | 3 |
| α-helix | 232-235 | 4 | |
| α-helix | 242-258 | 17 | |
| α-helix | 265-267 | 3 | |
| α-helix | 268-273 | 6 | |
| α-helix | 307-309 | 3 | |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 332-341 | 10 | |
| α-helix | 346-348 | 3 | |
| α-helix | 352-356 | 5 | |
| α-helix | 359-366 | 8 | |
| α-helix | 371-377 | 7 | |
Chain B: 12 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 451 | 1 | 4 |
| β-strand | 462 | 1 | 4 |
| β-strand | 470-475 | 6 | 4 |
| β-strand | 479-484 | 6 | 4 |
| α-helix | 492-505 | 14 | |
| β-strand | 513 | 1 | 5 |
| β-strand | 516-520 | 5 | 4 |
| β-strand | 526-530 | 5 | 4 |
| β-strand | 536 | 1 | 5 |
| α-helix | 537-542 | 6 | |
| α-helix | 550-569 | 20 | |
| β-strand | 572-573 | 2 | 6 |
| α-helix | 579-581 | 3 | |
| β-strand | 582-585 | 4 | 5 |
| β-strand | 589-592 | 4 | 5 |
| β-strand | 599-600 | 2 | 6 |
| β-strand | 616 | 1 | 3 |
| α-helix | 617-619 | 3 | |
| α-helix | 622-626 | 5 | |
| α-helix | 635-651 | 17 | |
| α-helix | 662-671 | 10 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 707-718 | 12 | |
Chain C: 16 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 451 | 1 | 7 |
| α-helix | 452-453 | 2 | |
| β-strand | 458-462 | 5 | 7 |
| β-strand | 471-475 | 5 | 7 |
| β-strand | 479-485 | 7 | 7 |
| α-helix | 492-505 | 14 | |
| β-strand | 513 | 1 | 8 |
| β-strand | 516-520 | 5 | 7 |
| β-strand | 525-530 | 6 | 7 |
| α-helix | 531-533 | 3 | |
| β-strand | 534-536 | 3 | 8 |
| α-helix | 537-538 | 2 | |
| α-helix | 539-543 | 5 | |
| α-helix | 550-569 | 20 | |
| β-strand | 572-573 | 2 | 9 |
| α-helix | 579-581 | 3 | |
| β-strand | 582-585 | 4 | 8 |
| β-strand | 589-592 | 4 | 8 |
| β-strand | 599-600 | 2 | 9 |
| β-strand | 616 | 1 | 10 |
| α-helix | 617-619 | 3 | |
| α-helix | 622-626 | 5 | |
| β-strand | 629 | 1 | 11 |
| α-helix | 635-651 | 17 | |
| α-helix | 662-671 | 10 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 705-706 | 2 | |
| α-helix | 707-718 | 12 | |
Chain D: 17 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 68-77 | 10 | 12 |
| β-strand | 80-87 | 8 | 12 |
| β-strand | 92-100 | 9 | 12 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| β-strand | 126 | 1 | 13 |
| β-strand | 129-134 | 6 | 12 |
| β-strand | 138-143 | 6 | 12 |
| β-strand | 150 | 1 | 13 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-184 | 22 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 13 |
| β-strand | 204-206 | 3 | 13 |
| α-helix | 213-218 | 6 | |
| β-strand | 223 | 1 | 10 |
| α-helix | 232-235 | 4 | |
| α-helix | 242-258 | 17 | |
| α-helix | 265-266 | 2 | |
| α-helix | 268-272 | 5 | |
| 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 | 371-378 | 8 | |
Chain E: 19 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-67 | 3 | |
| β-strand | 68-76 | 9 | 14 |
| β-strand | 80-87 | 8 | 14 |
| β-strand | 93-100 | 8 | 14 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-118 | 3 | |
| β-strand | 126 | 1 | 15 |
| β-strand | 129-134 | 6 | 14 |
| β-strand | 138-143 | 6 | 14 |
| β-strand | 149-150 | 2 | 15 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-179 | 17 | |
| α-helix | 180-184 | 5 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 15 |
| β-strand | 204-206 | 3 | 15 |
| α-helix | 213-218 | 6 | |
| β-strand | 223 | 1 | 16 |
| α-helix | 232-235 | 4 | |
| α-helix | 243-258 | 16 | |
| α-helix | 265-267 | 3 | |
| α-helix | 268-272 | 5 | |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 325-326 | 2 | |
| α-helix | 332-342 | 11 | |
| α-helix | 352-356 | 5 | |
| α-helix | 359-366 | 8 | |
| α-helix | 371-377 | 7 | |
Chain F: 12 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 451 | 1 | 17 |
| β-strand | 458-462 | 5 | 17 |
| β-strand | 471-475 | 5 | 17 |
| β-strand | 479-484 | 6 | 17 |
| α-helix | 492-505 | 14 | |
| β-strand | 513 | 1 | 18 |
| β-strand | 516-520 | 5 | 17 |
| β-strand | 526-530 | 5 | 17 |
| β-strand | 536 | 1 | 18 |
| α-helix | 537-542 | 6 | |
| α-helix | 550-569 | 20 | |
| β-strand | 572-573 | 2 | 19 |
| α-helix | 579-581 | 3 | |
| β-strand | 582-585 | 4 | 18 |
| β-strand | 589-592 | 4 | 18 |
| β-strand | 599-600 | 2 | 19 |
| β-strand | 616 | 1 | 16 |
| α-helix | 617-619 | 3 | |
| α-helix | 622-626 | 5 | |
| β-strand | 629 | 1 | 11 |
| α-helix | 635-651 | 17 | |
| α-helix | 662-671 | 10 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 707-718 | 12 | |
Chain G: 13 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 451 | 1 | 20 |
| β-strand | 458-462 | 5 | 20 |
| β-strand | 471-475 | 5 | 20 |
| β-strand | 479-484 | 6 | 20 |
| α-helix | 492-506 | 15 | |
| β-strand | 513 | 1 | 21 |
| β-strand | 516-520 | 5 | 20 |
| β-strand | 526-530 | 5 | 20 |
| β-strand | 536 | 1 | 21 |
| α-helix | 537-542 | 6 | |
| α-helix | 550-569 | 20 | |
| β-strand | 572-573 | 2 | 22 |
| α-helix | 579-581 | 3 | |
| β-strand | 582-585 | 4 | 21 |
| β-strand | 589-592 | 4 | 21 |
| β-strand | 599-600 | 2 | 22 |
| β-strand | 616 | 1 | 23 |
| α-helix | 617-619 | 3 | |
| α-helix | 622-626 | 5 | |
| α-helix | 635-651 | 17 | |
| α-helix | 662-670 | 9 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 705-706 | 2 | |
| α-helix | 707-718 | 12 | |
Chain H: 18 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 68-76 | 9 | 24 |
| β-strand | 80-87 | 8 | 24 |
| β-strand | 93-100 | 8 | 24 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| β-strand | 126 | 1 | 25 |
| β-strand | 129-134 | 6 | 24 |
| β-strand | 138-143 | 6 | 24 |
| β-strand | 149-150 | 2 | 25 |
| α-helix | 151-157 | 7 | |
| α-helix | 163-179 | 17 | |
| α-helix | 180-184 | 5 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 25 |
| β-strand | 204-206 | 3 | 25 |
| α-helix | 213-219 | 7 | |
| β-strand | 223 | 1 | 23 |
| α-helix | 224-225 | 2 | |
| α-helix | 232-235 | 4 | |
| α-helix | 243-258 | 16 | |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 325-326 | 2 | |
| α-helix | 332-341 | 10 | |
| α-helix | 346-348 | 3 | |
| α-helix | 352-357 | 6 | |
| α-helix | 359-365 | 7 | |
| α-helix | 371-378 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Dual specificity mitogen-activated protein kinase kinase 1 | A, D, E, H | protein | 341 | Homo sapiens | Q02750 (AlphaFold model) |
| Serine/threonine-protein kinase B-raf | B, C, F, G | protein | 308 | Homo sapiens | P15056 (AlphaFold model) |
Sequence of entity 1 (A, D, E, H), FASTA
>4MNE_1 Dual specificity mitogen-activated protein kinase kinase 1 (chains A, D, E, H)
MELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHE
CNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYL
REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHY
SVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSY
GMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAF
IKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGVLEHHHHHH
Sequence of entity 2 (B, C, F, G), FASTA
>4MNE_2 Serine/threonine-protein kinase B-raf (chains B, C, F, G)
MDRGSHHHHHHGSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGD
VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYH
HLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAT
VKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNI
NNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR
SLPKIHRK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 4 |
| 573 | 7-fluoro-3-[(2-fluoro-4-iodophenyl)amino]-N-{[(2S)-2-hydroxypropyl]oxy}furo[3,2… | C17 H14 F2 I N3 O4 | 5 |
| ACP | Phosphomethylphosphonic acid adenylate ester | C11 H18 N5 O12 P3 | 4 |
Water and common crystallization additives (CL) are not listed.
Primary citation
Structure of the BRAF-MEK Complex Reveals a Kinase Activity Independent Role for BRAF in MAPK Signaling. Haling, J.R., Sudhamsu, J., Yen, I. et al. Cancer Cell (2014) 26:402-413. DOI 10.1016/j.ccr.2014.07.007 · PubMed
Other PDB entries of the same protein (UniProt Q02750 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7B7R 1.7 Å, MEK1 in complex with compound 4
- 7B9L 1.7 Å, MEK1 in complex with compound 23
- 3EQC 1.8 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
- 3EQI 1.9 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
- 3EQH 2.0 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
- 3VVH 2.0 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex…
- 7B94 2.0 Å, MEK1 in complex with compound 6
- 7F2X 2.01 Å, Crystal structure of MEK1 C121S mutant
- 9AXX 2.07 Å, Crystal structure of BRAF/MEK1 complex with NST-628 and an active RAF dimer
- 3EQD 2.1 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
- 4AN3 2.1 Å, Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518…
- 7XLP 2.1 Å, MEK1 bound to DS03090629
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