← Back to search
7umb

NanoBRET tracer Tram-bo bound to a KSR2-MEK1 complex

Method: X-RAY DIFFRACTION Dmax: 86.8 Å Quality: EXCELLENT
▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Kinase suppressor of Ras 2

Homo sapiens

UniProt Q6VAB6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 634–950 Not recorded Dual specificity mitogen-activated protein kinase kinase 1 × 1 （Q02750） ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 U9F {3-[(1M,2M)-2-{[(1S,2P)-1H,1'H-[2,2'-bipyrrol]-5-yl-kappaN~1~]methylidene}-2H-pyrrol-5-yl-kappaN]-N-(2-{2-[3-({(3M)-3-[(4aM)-3-cyclopropyl-5-(2-fluoro-4-iodoanilino)-6,8-dimethyl-2,4,7-trioxo-3,4,6,7-tetrahydropyrido[4,3-d]pyrimidin-1(2H)-yl]phenyl}amino)-3-oxopropoxy]ethoxy}ethyl)propanamidato}(difluorido)boron × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate Resolution 3.23 Å R-free 0.268

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 7UMB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2Y4I KSR2-MEK1 heterodimer Deposited 2011-01-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa） Fragment：KINASE DOMAIN, RESIDUES 634-950
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.25；293 K；12% (W/V) PEG 3350, 0.2 M NA CITRATE, 10 MM PR ACETATE, BIS-TRIS PROPANE PH 6.25.
Resolution 3.46 Å R-free 0.293
5KKR KSR2:MEK1 Complex Bound to the Small Molecule APS-2-79 Deposited 2016-06-22 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 634–950（317 aa）
Not recorded 6U7 6,7-dimethoxy-~{N}-(2-methyl-4-phenoxy-phenyl)quinazolin-4-amine × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.25；293 K；12% PEG-3350 100mM Bis-Tris 200mM Sodium Citrate 10mM Magnesium Acetate
Resolution 3.51 Å R-free 0.287
5KKR KSR2:MEK1 Complex Bound to the Small Molecule APS-2-79 Deposited 2016-06-22 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded 6U7 6,7-dimethoxy-~{N}-(2-methyl-4-phenoxy-phenyl)quinazolin-4-amine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.25；293 K；12% PEG-3350 100mM Bis-Tris 200mM Sodium Citrate 10mM Magnesium Acetate
Resolution 3.51 Å R-free 0.287
7JUQ Crystal Structure of KSR2:MEK1 in complex with ADP Deposited 2020-08-20 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate
Resolution 3.22 Å R-free 0.288
7JUR Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor Trametinib Deposited 2020-08-20 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 QOM Trametinib × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；12% PEG-3350, 100 mM MES pH 6.25, 200 mM Magnesium Acetate
Resolution 2.82 Å R-free 0.277
7JUS Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor Cobimetinib Deposited 2020-08-20 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 VKD Cobimetinib × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate
Resolution 2.99 Å R-free 0.265
7JUT Crystal Structure of KSR2:MEK1 in complex with ANP-PNP, and allosteric MEK inhibitor Selumetinib Deposited 2020-08-20 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 3EW 5-[(4-bromo-2-chlorophenyl)amino]-4-fluoro-N-(2-hydroxyethoxy)-1-methyl-1H-benzimidazole-6-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate
Resolution 3.09 Å R-free 0.300
7JUU Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor PD0325901 Deposited 2020-08-20 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate
Resolution 3.19 Å R-free 0.258
7JUV Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor APS-9-95-1 Deposited 2020-08-20 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 634–950（317 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 VKG N-(3-{3-cyclopropyl-5-[(2-fluoro-4-iodophenyl)amino]-6,8-dimethyl-2,4,7-trioxo-3,4,6,7-tetrahydropyrido[4,3-d]pyrimidin-1(2H)-yl}phenyl)-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate
Resolution 3.36 Å R-free 0.255

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KSR2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain B； PDBConstruct 26–342； UniProt 634–950

Dual specificity mitogen-activated protein kinase kinase 1

Homo sapiens

UniProt Q02750

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 35–393 Not recorded Kinase suppressor of Ras 2 × 1 （Q6VAB6） ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 U9F {3-[(1M,2M)-2-{[(1S,2P)-1H,1'H-[2,2'-bipyrrol]-5-yl-kappaN~1~]methylidene}-2H-pyrrol-5-yl-kappaN]-N-(2-{2-[3-({(3M)-3-[(4aM)-3-cyclopropyl-5-(2-fluoro-4-iodoanilino)-6,8-dimethyl-2,4,7-trioxo-3,4,6,7-tetrahydropyrido[4,3-d]pyrimidin-1(2H)-yl]phenyl}amino)-3-oxopropoxy]ethoxy}ethyl)propanamidato}(difluorido)boron × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；PEG 2000, MES, pH 6.5, Magnesium acetate Resolution 3.23 Å R-free 0.268

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 7UMB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1S9J X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP Deposited 2004-02-04 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 61–392（332 aa）
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 BBM 5-BROMO-N-(2,3-DIHYDROXYPROPOXY)-3,4-DIFLUORO-2-[(2-FLUORO-4-IODOPHENYL)AMINO]BENZAMIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；288 K；PEG8K, Ammonium phosphate, Imidazole-malate, DTT, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.40 Å R-free 0.269
2P55 X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP Deposited 2007-03-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–393（332 aa）
Not recorded MG MAGNESIUM ION × 2 MRA 2-[(4-ETHYNYL-2-FLUOROPHENYL)AMINO]-3,4-DIFLUORO-N-(2-HYDROXYETHOXY)BENZAMIDE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å R-free 0.301
3DV3 MEK1 with PF-04622664 Bound Deposited 2008-07-18 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–382（321 aa） Fragment：UNP residues 62-382
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MEK 3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-5-[(2-hydroxyethoxy)methyl]benzamide × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.30 Å R-free 0.221
3DV3 MEK1 with PF-04622664 Bound Deposited 2008-07-18 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–382（321 aa） Fragment：UNP residues 62-382
Not recorded MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MEK 3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-5-[(2-hydroxyethoxy)methyl]benzamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 2.30 Å R-free 0.221
3DY7 X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP Deposited 2008-07-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：Protein Kinase Domain, UNP residues 62-393
Not recorded MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 1CX (5S)-4,5-difluoro-6-[(2-fluoro-4-iodophenyl)imino]-N-(2-hydroxyethoxy)cyclohexa-1,3-diene-1-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；288 K；PEG8K, Ammonium phosphate, Imidazole-malate, DTT, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.70 Å R-free 0.269
3E8N X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) complexed with a potent inhibitor RDEA119 and MgATP Deposited 2008-08-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa）
Not recorded MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 VRA N-{3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-6-methoxyphenyl}-1-[(2S)-2,3-dihydroxypropyl]cyclopropanesulfonamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；277 K；20 mM HEPES, 150 mM NH4H2PO4, 0.5 mM EDTA, 2 mM TCEP, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.252
3E8N X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) complexed with a potent inhibitor RDEA119 and MgATP Deposited 2008-08-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–393（332 aa）
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 VRA N-{3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-6-methoxyphenyl}-1-[(2S)-2,3-dihydroxypropyl]cyclopropanesulfonamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；277 K；20 mM HEPES, 150 mM NH4H2PO4, 0.5 mM EDTA, 2 mM TCEP, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.252
3EQB X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a complex with ligand and MgATP Deposited 2008-09-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–393（332 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 LUG N-(5-{3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]phenyl}-1,3,4-oxadiazol-2-yl)ethane-1,2-diamine × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.62 Å R-free 0.264
3EQC X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a ternary complex with compound 1, ATP-GS AND MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F 3BM 2-[(2-chloro-4-iodophenyl)amino]-N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluorobenzamide × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 1.80 Å R-free 0.235
3EQC X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a ternary complex with compound 1, ATP-GS AND MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F 3BM 2-[(2-chloro-4-iodophenyl)amino]-N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluorobenzamide × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 1.80 Å R-free 0.235
3EQD X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with ATP-GS and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.10 Å
3EQD X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with ATP-GS and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.10 Å
3EQF X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with K252A and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F KSA K-252A × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.70 Å
3EQF X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with K252A and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F KSA K-252A × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.70 Å
3EQG X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a ternary complex with PD, ADP AND MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 NA SODIUM ION × 1 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.50 Å R-free 0.273
3EQG X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a ternary complex with PD, ADP AND MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 2 NA SODIUM ION × 2 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.50 Å R-free 0.273
3EQH X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a ternary complex with U0126, ADP and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F 5BM (2Z)-bis{amino[(2-aminophenyl)sulfanyl]methylidene}butanedinitrile × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.00 Å
3EQH X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a ternary complex with U0126, ADP and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F 5BM (2Z)-bis{amino[(2-aminophenyl)sulfanyl]methylidene}butanedinitrile × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 2.00 Å
3EQI X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with ADP and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 1.90 Å
3EQI X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with ADP and MG2P Deposited 2008-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 35–393（359 aa） Fragment：Protein kinase domain, UNP residues 35-393
Mutation：S265N, S266K, Y267F ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1M TRIS-CL, pH 8.0; 18% PEG 4000; 0.2M CALCIUM CHLORIDE; 3% DMSO, VAPOR DIFFUSION HANGING DROP, temperature 281K
Resolution 1.90 Å
3MBL Crystal Structure of the human mitogen-activated protein kinase kinase 1 (MEK 1) in complex with ligand and MgADP Deposited 2010-03-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–382（321 aa） Fragment：Kinase Domain
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 LSG 5-acetyl-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-1-methyl-1H-pyrrole-3-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.60 Å R-free 0.215
3MBL Crystal Structure of the human mitogen-activated protein kinase kinase 1 (MEK 1) in complex with ligand and MgADP Deposited 2010-03-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–382（321 aa） Fragment：Kinase Domain
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 LSG 5-acetyl-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-1-methyl-1H-pyrrole-3-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.60 Å R-free 0.215
3ORN Mitogen-activated protein kinase kinase 1 (MEK1) in complex with CH4987655 and MgAMP-PNP Deposited 2010-09-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–270（209 aa） Fragment：UNP RESIDUES 62-270, 303-393
Chain A 303–393（91 aa） Fragment：UNP RESIDUES 62-270, 303-393
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 3OR 3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-5-[(3-oxo-1,2-oxazinan-2-yl)methyl]benzamide × 1 PGE TRIETHYLENE GLYCOL × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2M Ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.277
3ORN Mitogen-activated protein kinase kinase 1 (MEK1) in complex with CH4987655 and MgAMP-PNP Deposited 2010-09-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–270（209 aa） Fragment：UNP RESIDUES 62-270, 303-393
Chain A 303–393（91 aa） Fragment：UNP RESIDUES 62-270, 303-393
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 3OR 3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-5-[(3-oxo-1,2-oxazinan-2-yl)methyl]benzamide × 2 PGE TRIETHYLENE GLYCOL × 2 SO4 SULFATE ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2M Ammonium sulfate, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.80 Å R-free 0.277
3OS3 Mitogen-activated protein kinase kinase 1 (MEK1) in complex with CH4858061 and MgATP Deposited 2010-09-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–270（209 aa） Fragment：UNP RESIDUES 62-270, 303-393
Chain A 303–393（91 aa） Fragment：UNP RESIDUES 62-270, 303-393
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 3OS 2-[(4-ethynyl-2-fluorophenyl)amino]-3,4-difluoro-N-(2-hydroxyethoxy)-5-{[(2-hydroxyethoxy)imino]methyl}benzamide × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；277 K；7.5-10% PEG 8000, 0.2M NaCl, 0.2M Ammonium sulfate, 0.1M citrate buffer, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.80 Å R-free 0.356
3OS3 Mitogen-activated protein kinase kinase 1 (MEK1) in complex with CH4858061 and MgATP Deposited 2010-09-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–270（209 aa） Fragment：UNP RESIDUES 62-270, 303-393
Chain A 303–393（91 aa） Fragment：UNP RESIDUES 62-270, 303-393
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 3OS 2-[(4-ethynyl-2-fluorophenyl)amino]-3,4-difluoro-N-(2-hydroxyethoxy)-5-{[(2-hydroxyethoxy)imino]methyl}benzamide × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；277 K；7.5-10% PEG 8000, 0.2M NaCl, 0.2M Ammonium sulfate, 0.1M citrate buffer, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.80 Å R-free 0.356
3PP1 Crystal Structure of the Human Mitogen-activated protein kinase kinase 1 (MEK 1) in complex with ligand and MgATP Deposited 2010-11-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–382（321 aa） Fragment：kinase domain
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 IZG 3-[(2R)-2,3-dihydroxypropyl]-6-fluoro-5-[(2-fluoro-4-iodophenyl)amino]-8-methylpyrido[2,3-d]pyrimidine-4,7(3H,8H)-dione × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；10% MPD, 0.1M MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.70 Å R-free 0.219
3SLS Crystal Structure of human MEK-1 kinase in complex with UCB1353770 and AMPPNP Deposited 2011-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 45–383（339 aa） Fragment：MEK-1 F11 fragment
Mutation：delta 264-307 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 77D 2-[(2-fluoro-4-iodophenyl)amino]-5,5-dimethyl-8-oxo-N-[(3R)-piperidin-3-yl]-5,6,7,8-tetrahydro-4H-thieno[2,3-c]azepine-3-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；18% PEG-3350, 200mM Ammonium fluoride, 4% Glycerol, 10mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.30 Å R-free 0.287
3SLS Crystal Structure of human MEK-1 kinase in complex with UCB1353770 and AMPPNP Deposited 2011-06-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 45–383（339 aa） Fragment：MEK-1 F11 fragment
Mutation：delta 264-307 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 77D 2-[(2-fluoro-4-iodophenyl)amino]-5,5-dimethyl-8-oxo-N-[(3R)-piperidin-3-yl]-5,6,7,8-tetrahydro-4H-thieno[2,3-c]azepine-3-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；18% PEG-3350, 200mM Ammonium fluoride, 4% Glycerol, 10mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.30 Å R-free 0.287
3V01 Discovery of Novel Allosteric MEK Inhibitors Possessing Classical and Non-classical Bidentate Ser212 Interactions. Deposited 2011-12-07 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：UNP residues 62-393
Not recorded 3V0 N-{[(2R)-2,3-dihydroxypropyl]oxy}-3-[(2-fluoro-4-iodophenyl)amino]furo[3,2-c]pyridine-2-carboxamide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；286 K；16-20% w/v PEG8K, 0.1M HEPES, 250mM NH4H2PO4, 1mM TCEP, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 286K
Resolution 2.71 Å R-free 0.240
3V04 Discovery of Novel Allosteric MEK Inhibitors Possessing Classical and Non-classical Bidentate Ser212 Interactions. Deposited 2011-12-07 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：UNP residues 62-393
Not recorded V04 4-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-1H-indazole-5-carboxamide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；286 K；16-20 %w/v PEG8K, 0.1M HEPES, 250mM NH4H2PO4, 1mM TCEP, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 286K
Resolution 2.70 Å R-free 0.243
3VVH X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex with an inhibitor and MgATP Deposited 2012-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：UNP RESIDUES 62-393
Not recorded MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；279 K；PEG 4000, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 279K
Resolution 2.00 Å R-free 0.225
3VVH X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex with an inhibitor and MgATP Deposited 2012-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 62–393（332 aa） Fragment：UNP RESIDUES 62-393
Not recorded MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；279 K；PEG 4000, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 279K
Resolution 2.00 Å R-free 0.225
3VVH X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex with an inhibitor and MgATP Deposited 2012-07-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 62–393（332 aa） Fragment：UNP RESIDUES 62-393
Not recorded MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；279 K；PEG 4000, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 279K
Resolution 2.00 Å R-free 0.225
3W8Q Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1) Deposited 2013-03-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 39–382（344 aa） Fragment：kinase domain, UNP residues 39-382
Mutation：T292A, S298A AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277 K；16%(w/v) PEG 3350, 0.1M ammonium citrate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277.0K
Resolution 2.20 Å R-free 0.268
3WIG Human MEK1 kinase in complex with CH5126766 and MgAMP-PNP Deposited 2013-09-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–270（209 aa）
Chain A 303–393（91 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 PG4 TETRAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；277 K；7.5-10% PEG 8000, 0.2M NaCl, 0.2M Ammonium sulfate, 0.1M citrate buffer, pH 4.2, vapor diffusion, sitting drop, temperature 277K
Resolution 2.70 Å R-free 0.250
3WIG Human MEK1 kinase in complex with CH5126766 and MgAMP-PNP Deposited 2013-09-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–270（209 aa）
Chain A 303–393（91 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 2 PG4 TETRAETHYLENE GLYCOL × 2 CL CHLORIDE ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.2；277 K；7.5-10% PEG 8000, 0.2M NaCl, 0.2M Ammonium sulfate, 0.1M citrate buffer, pH 4.2, vapor diffusion, sitting drop, temperature 277K
Resolution 2.70 Å R-free 0.250
3ZLS Crystal structure of MEK1 in complex with fragment 6 Deposited 2013-02-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa） Fragment：RESIDUES 37-383
Mutation：YES 92P 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBOXYLIC ACID × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.7；pH 7.7
Resolution 2.50 Å R-free 0.234
3ZLW Crystal structure of MEK1 in complex with fragment 3 Deposited 2013-02-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa）
Mutation：YES MT8 (1R)-1-hydroxy-1-methyl-2,3,6,7-tetrahydro-1H,5H-pyrido[3,2,1-ij]quinolin-5-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.7；pH 7.7
Resolution 2.12 Å R-free 0.248
3ZLX Crystal structure of MEK1 in complex with fragment 18 Deposited 2013-02-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa）
Mutation：YES 5EZ 7-choro-6-[(3R)-pyrrolidin-3-ylmethoxy]isoquinolin-1(2H)-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.7；Appropriate single crystals were grown using this set-up in PEG 4000 18%, Tris 100mM pH7.7, DMSO 2% and CaCl2 0.2M and were extracted from the low volume drops, cryo-protected in mother liquor with 20% glycerol and flash cooled for synchrotron collection
Resolution 2.20 Å R-free 0.236
3ZLY Crystal structure of MEK1 in complex with fragment 8 Deposited 2013-02-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa） Fragment：RESIDUES 37-383
Mutation：YES YSO 3-AMINO-1H-INDAZOLE-4-CARBONITRILE × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.7；Appropriate single crystals were grown using this set-up in PEG 4000 18%, Tris 100mM pH7.7, DMSO 2% and CaCl2 0.2M and were extracted from the low volume drops, cryo-protected in mother liquor with 20% glycerol and flash cooled for synchrotron collection
Resolution 2.11 Å R-free 0.248
3ZM4 Crystal structure of MEK1 in complex with fragment 1 Deposited 2013-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa） Fragment：RESIDUES 37-383
Mutation：YES 22T 7-chloranyl-6-[(3S)-pyrrolidin-3-yl]oxy-2H-isoquinolin-1-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.7；Appropriate single crystals were grown using this set-up in PEG 4000 18%, Tris 100mM pH7.7, DMSO 2% and CaCl2 0.2M and were extracted from the low volume drops, cryo-protected in mother liquor with 20% glycerol and flash cooled for synchrotron collection
Resolution 2.37 Å R-free 0.241
4AN2 Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs. Deposited 2012-03-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 61–262（202 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Chain A 305–392（88 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Mutation：YES Mutation：YES EUI [3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]-[3-OXIDANYL-3-[(2S)-PIPERIDIN-2-YL]AZETIDIN-1-YL]METHANONE × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.9；MEK1 (8 MG/ML) WAS INCUBATED WITH INHIBITOR (300 MICROMOLAR FINAL CONCENTRATION) AND AMPPCP (2.8 MM FINAL CONCENTRATION) FOR TWO HOURS ON ICE, FOLLOWED BY CRYSTALLIZION VS. 26.5% PEG-2000 MME, 0.1 M TRIMETHYLAMINE N- OXIDE AND 0.1 M TRIS (PH 8.9)
Resolution 2.50 Å R-free 0.299
4AN3 Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs. Deposited 2012-03-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 61–262（202 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Chain A 305–392（88 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Mutation：YES Mutation：YES MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 5Y0 N-[(2S)-2,3-bis(oxidanyl)propoxy]-3,4-bis(fluoranyl)-2-[(2-fluoranyl-4-iodanyl-phenyl)amino]benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.9；SITTING DROP VAPOR DIFFUSION VS. 26.5 % PEG-2000 MME, 0.1 M TRIMETHYLAMINE N-OXIDE, 0.1 M TRIS (PH 8.9)
Resolution 2.10 Å R-free 0.283
4AN9 Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs. Deposited 2012-03-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 61–262（202 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Chain A 305–392（88 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Mutation：YES Mutation：YES ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 2P7 [3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]-(3-OXIDANYLAZETIDIN-1-YL)METHANONE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.9；SITTING DROP VAPOR-DIFFUSION VS. 26.5 % PEG-2000 MME, 0.1 M TRIMETHYLAMINE N-OXIDE, 0.1 M TRIS (PH 8.9)
Resolution 2.80 Å R-free 0.313
4ANB Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs. Deposited 2012-03-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 61–262（202 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Chain A 305–392（88 aa） Fragment：PROTEIN KINASE DOMAIN, RESIDUES 61-262,305-392
Mutation：YES Mutation：YES YQY [3-(AMINOMETHYL)-3-OXIDANYL-AZETIDIN-1-YL]-[3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]METHANONE × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.9；SITTING DROP VAPOR DIFFUSION VS. 26.5 % PEG-2000 MME, 0.1 M TRIMETHYLAMINE N-OXIDE, 0.1 M TRIS (PH 8.9)
Resolution 2.20 Å R-free 0.296
4ARK CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN MAP KINASE KINASE 1 (MEK1) IN COMPLEX WITH A SMALL MOLECULE INHIBITOR AND ADP Deposited 2012-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–393（332 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 62-393
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 M3K 2-([3R-3,4-dihydroxybutyl]oxy)-4-fluoro-6-[(2-fluoro-4-iodophenyl)amino]benzamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions 0.1 M IMIDAZOLE-MALATE, 300 MM(NH4)H2PO4, 13% PEG 8000, PH 5.8
Resolution 2.60 Å R-free 0.211
4LMN Crystal Structure of MEK1 kinase bound to GDC0973 Deposited 2013-07-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：Kinase domain (UNP residues 62-393)
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 EUI [3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]-[3-OXIDANYL-3-[(2S)-PIPERIDIN-2-YL]AZETIDIN-1-YL]METHANONE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；12% w/v PEG 8000, 0.4M NH4H2PO4, 0.1M HEPES, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.233
4LMN Crystal Structure of MEK1 kinase bound to GDC0973 Deposited 2013-07-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 62–393（332 aa） Fragment：Kinase domain (UNP residues 62-393)
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 EUI [3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]-[3-OXIDANYL-3-[(2S)-PIPERIDIN-2-YL]AZETIDIN-1-YL]METHANONE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；12% w/v PEG 8000, 0.4M NH4H2PO4, 0.1M HEPES, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.80 Å R-free 0.233
4MNE Crystal structure of the BRAF:MEK1 complex Deposited 2013-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 62–393（332 aa） Fragment：UNP residues 62-393
Chain D 62–393（332 aa） Fragment：UNP residues 62-393
Not recorded ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 573 7-fluoro-3-[(2-fluoro-4-iodophenyl)amino]-N-{[(2S)-2-hydroxypropyl]oxy}furo[3,2-c]pyridine-2-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；292 K；20% PEG8000, 0.1 M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.85 Å R-free 0.240
4MNE Crystal structure of the BRAF:MEK1 complex Deposited 2013-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 62–393（332 aa） Fragment：UNP residues 62-393
Chain H 62–393（332 aa） Fragment：UNP residues 62-393
Not recorded ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 573 7-fluoro-3-[(2-fluoro-4-iodophenyl)amino]-N-{[(2S)-2-hydroxypropyl]oxy}furo[3,2-c]pyridine-2-carboxamide × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；292 K；20% PEG8000, 0.1 M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 2.85 Å R-free 0.240
4U7Z Mitogen-Activated Protein Kinase Kinase (MEK1) bound to G805 Deposited 2014-07-31 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：kinase domain (UNP residues 62-393)
Not recorded MG MAGNESIUM ION × 1 3EW 5-[(4-bromo-2-chlorophenyl)amino]-4-fluoro-N-(2-hydroxyethoxy)-1-methyl-1H-benzimidazole-6-carboxamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；The protein was concentrated to 15mg/ml and incubated with 10 fold molar excess inhibitor plus 1mM MgAMP-PNP before crystallization. MEK1 crystals grew from hanging drop vapor diffusion using 12% w/v PEG 8000, 0.4M NH4H2PO4 and 0.1M HEPES pH 6.9 at 18 degC.
Resolution 2.81 Å R-free 0.214
4U80 MEK 1 kinase bound to G799 Deposited 2014-07-31 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：Kinase domain (UNP residues 62-393)
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 3EX 3-[(4-cyclopropyl-2-fluorophenyl)amino]-N-(2-hydroxyethoxy)furo[3,2-c]pyridine-2-carboxamide × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；The protein was concentrated to 15mg/m1 and incubated with 10 fold molar excess inhibitor plus 1mM MgAMP-PNP before crystallization. MEK1 crystals grew from hanging drop vapor diffusion using 12% w/v PEG 8000, 0.4M NH4H2PO4 and 0.1M HEPES pH 6.9 at 18 degC .
Resolution 2.80 Å R-free 0.224
4U81 MEK1 Kinase bound to small molecule inhibitor G659 Deposited 2014-07-31 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 62–393（332 aa） Fragment：Kinase domain (UNP residues 62-393)
Not recorded MG MAGNESIUM ION × 1 3EY 8-[(4-cyclopropyl-2-fluorophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-7-carboxamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；The protein was concentrated to 15mg/ml and incubated with 10 fold molar excess inhibitor plus 1mM MgAMP-PNP before crystallization. MEK1 crystals grew from hanging drop vapor diffusion using 12% w/v PEG 8000, 0.4M NH4H2PO4 and 0.1M HEPES pH 6.9 at 18 degC.
Resolution 2.70 Å R-free 0.218
5BX0 An Automated Microscale Thermophoresis Screening Approach for Fragment-Based Lead Discovery Deposited 2015-06-08 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa） Fragment：residues 37-383
Not recorded 4W5 ethyl 2H-indazole-5-carboxylate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7.65；277 K；PEG4000 20% CaCl2 200mM Glycerol 25% ph7.7
Resolution 2.93 Å R-free 0.252
5EYM MEK1 IN COMPLEX WITH BI 847325 Deposited 2015-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–393（359 aa） Fragment：UNP residues 35-393
Mutation：S298N, S299K, Y300F 5U5 3-[(3~{Z})-3-[[[4-[(dimethylamino)methyl]phenyl]amino]-phenyl-methylidene]-2-oxidanylidene-1~{H}-indol-6-yl]-~{N}-ethyl-prop-2-ynamide × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；18 % PEG 4000, 100 mM Tris, 300 mM NaCl
Resolution 2.70 Å R-free 0.308
5EYM MEK1 IN COMPLEX WITH BI 847325 Deposited 2015-11-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 35–393（359 aa） Fragment：UNP residues 35-393
Mutation：S298N, S299K, Y300F 5U5 3-[(3~{Z})-3-[[[4-[(dimethylamino)methyl]phenyl]amino]-phenyl-methylidene]-2-oxidanylidene-1~{H}-indol-6-yl]-~{N}-ethyl-prop-2-ynamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；18 % PEG 4000, 100 mM Tris, 300 mM NaCl
Resolution 2.70 Å R-free 0.308
5HZE Mek1 adopts DFG-out conformation when bound to an analog of E6201. Deposited 2016-02-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa）
Mutation：S298N, S299K, Y300F E62 (3S,4R,8S,9S,11E)-8,9,16-trihydroxy-3,4-dimethyl-14-(methylamino)-3,4,5,6,9,10-hexahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione × 1 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；0.1 M Tris pH 8.0, 180 mM CaCl2, 14-18% PEG 4000. Co-crystallized with 1mM ATPgammaS (30 mM stock formulated in H2O). Crystals backsoaked for 2 weeks in 1 mM compound 3.3% DMSO final.
Resolution 2.40 Å R-free 0.287
5YT3 Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D mutant Deposited 2017-11-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 39–382（344 aa）
Chain B 39–382（344 aa）
Mutation：S218D,S222D,T292A,S298A Mutation：S218D,S222D,T292A,S298A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1M HEPES, 12%(w/v) PEG3350, 0.1M ammonium citrate,
Resolution 2.90 Å R-free 0.289
5YT3 Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 S218D and S222D mutant Deposited 2017-11-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 39–382（344 aa）
Chain D 39–382（344 aa）
Mutation：S218D,S222D,T292A,S298A Mutation：S218D,S222D,T292A,S298A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；0.1M HEPES, 12%(w/v) PEG3350, 0.1M ammonium citrate,
Resolution 2.90 Å R-free 0.289
6NYB Structure of a MAPK pathway complex Deposited 2019-02-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–393（393 aa）
Mutation：S218A, S222A AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 ZN ZINC ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.10 Å
6PP9 Crystal structure of BRAF:MEK1 complex Deposited 2019-07-05 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 CL CHLORIDE ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；293 K；100 mM Bis-Tris pH 6.4, 200 mM Ammonium Sulfate, and 22% PEG3350
Resolution 2.59 Å R-free 0.245
6Q0J Structure of a MAPK pathway complex Deposited 2019-08-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 1–393（393 aa）
Chain D 1–393（393 aa）
Mutation：S218A, S222A Mutation：S218A, S222A MG MAGNESIUM ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.90 Å
6Q0T Structure of a MAPK pathway complex Deposited 2019-08-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain C 1–392（392 aa）
Mutation：S218A, S222A MG MAGNESIUM ION × 1 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.70 Å
6U2G BRAF-MEK complex with AMP-PCP bound to BRAF Deposited 2019-08-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2–393（392 aa）
Not recorded ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；Ammonium sulfate, MES, PEK 8000
Resolution 2.89 Å R-free 0.276
6V2W Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP Deposited 2019-11-25 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Bis-Tris pH 8.5, 200 mM Lithium Sulfate, and 22% PEG3350
Resolution 3.12 Å R-free 0.237
6X2P Crystal Structure of the Mek1NES peptide bound to CRM1 Deposited 2020-05-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 28–44（17 aa） Fragment：residues 28-44
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；273 K；17% (weight/vol) PEG3350, 100 mM Bis-Tris (pH 6.4), 200 mM ammonium nitrate, and 10 mM Spermine HCl
Resolution 2.40 Å R-free 0.252
6X2S Crystal Structure of Mek1(NQ)NES peptide bound to CRM Deposited 2020-05-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 29–44（16 aa） Fragment：residues 29-44
Mutation：D43N, E44Q GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；273 K；17% (weight/vol) PEG3350, 100 mM Bis-Tris (pH 6.4), 200 mM ammonium nitrate, and 10 mM Spermine HCl
Resolution 2.50 Å R-free 0.246
6X2X Crystal Structure of Mek1NES peptide bound to CRM1(E571K) Deposited 2020-05-21 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 29–44（16 aa） Fragment：residues 29-44
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；273 K；17% (weight/vol) PEG3350, 100 mM Bis-Tris (pH 6.4), 200 mM ammonium nitrate, and 10 mM Spermine HCl
Resolution 2.46 Å R-free 0.250
7B3M MEK1 in complex with compound 6 Deposited 2020-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Not recorded MG MAGNESIUM ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 SU5 1~{H}-indol-2-yl(pyridin-3-yl)methanone × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；MEK1 was prepared in buffer containing 25 mM Tris pH 7.5, 150 mM NaCl, 5% glycerol and 1 mM TCEP at a concentration of 10 mg/ml mixed with 2 mM MgCl2 and 2 mM AMP-PNP, and incubated at room temperature for 30 minutes. Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2 at room temperature.
Resolution 2.30 Å R-free 0.268
7B3M MEK1 in complex with compound 6 Deposited 2020-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 37–263（227 aa）
Chain B 308–383（76 aa）
Not recorded MG MAGNESIUM ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 SU5 1~{H}-indol-2-yl(pyridin-3-yl)methanone × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；MEK1 was prepared in buffer containing 25 mM Tris pH 7.5, 150 mM NaCl, 5% glycerol and 1 mM TCEP at a concentration of 10 mg/ml mixed with 2 mM MgCl2 and 2 mM AMP-PNP, and incubated at room temperature for 30 minutes. Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2 at room temperature.
Resolution 2.30 Å R-free 0.268
7B7R MEK1 in complex with compound 4 Deposited 2020-12-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 T1K 2-[5-[ethyl(methyl)amino]imidazo[1,2-a]pyrimidin-7-yl]phenol × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2
Resolution 1.70 Å R-free 0.218
7B7R MEK1 in complex with compound 4 Deposited 2020-12-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 37–263（227 aa）
Chain B 308–383（76 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 T1K 2-[5-[ethyl(methyl)amino]imidazo[1,2-a]pyrimidin-7-yl]phenol × 1 SO4 SULFATE ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2
Resolution 1.70 Å R-free 0.218
7B94 MEK1 in complex with compound 6 Deposited 2020-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 T3W 2-(4-iodophenyl)-8~{H}-imidazo[1,2-c]pyrimidin-5-one × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2
Resolution 2.00 Å R-free 0.265
7B94 MEK1 in complex with compound 6 Deposited 2020-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 37–263（227 aa）
Chain B 308–383（76 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 T3W 2-(4-iodophenyl)-8~{H}-imidazo[1,2-c]pyrimidin-5-one × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2
Resolution 2.00 Å R-free 0.265
7B9L MEK1 in complex with compound 23 Deposited 2020-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 T4N ~{N}-(4-methoxyphenyl)-2-[(2~{S})-3-oxidanylidenethiomorpholin-2-yl]ethanamide × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2
Resolution 1.70 Å R-free 0.214
7B9L MEK1 in complex with compound 23 Deposited 2020-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 37–263（227 aa）
Chain B 308–383（76 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 T4N ~{N}-(4-methoxyphenyl)-2-[(2~{S})-3-oxidanylidenethiomorpholin-2-yl]ethanamide × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Crystals were obtained from hanging drops by mixing a 1:1 ratio of protein solution with well solution containing 2 M AmSO4, 0.1 M NaCl and 0.1 M Bis-tris pH 6.1-6.2
Resolution 1.70 Å R-free 0.214
7M0T Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and Selumetinib Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A 3EW 5-[(4-bromo-2-chlorophenyl)amino]-4-fluoro-N-(2-hydroxyethoxy)-1-methyl-1H-benzimidazole-6-carboxamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Tris 8.5, 200 mM Lithium Sulfate and 22% PEG 3350
Resolution 3.19 Å R-free 0.254
7M0U Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and Binimetinib Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 QO7 5-[(4-bromo-2-fluorophenyl)amino]-4-fluoro-N-(2-hydroxyethoxy)-1-methyl-1H-benzimidazole-6-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Bis-Tris pH 8.5, 200 mM Lithium Sulfate, and 22% PEG3350
Resolution 3.09 Å R-free 0.230
7M0V Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and Cobimetinib Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 EUI [3,4-BIS(FLUORANYL)-2-[(2-FLUORANYL-4-IODANYL-PHENYL)AMINO]PHENYL]-[3-OXIDANYL-3-[(2S)-PIPERIDIN-2-YL]AZETIDIN-1-YL]METHANONE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Tris 8.5, 200 mM Lithium Sulfate and 22% PEG 3,350
Resolution 3.16 Å R-free 0.234
7M0W Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and Pimasertib Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 QOA N-[(2S)-2,3-dihydroxypropyl]-3-[(2-fluoro-4-iodophenyl)amino]pyridine-4-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100 mM Tris 8.5, 200 mM Lithium Sulfate and 22% PEG 3,350
Resolution 3.09 Å R-free 0.233
7M0X Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and PD0325901 Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 CL CHLORIDE ION × 1 4BM N-{[(2R)-2,3-dihydroxypropyl]oxy}-3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]benzamide × 1 SO4 SULFATE ION × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；293 K；100 mM Bis-Tris pH 6.4, 200 mM Ammonium Sulfate, and 22% PEG3350
Resolution 2.47 Å R-free 0.215
7M0Y Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and Trametinib Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 1 QOM Trametinib × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Tris 8.5, 200 mM Lithium Sulfate and 22% PEG 3,350
Resolution 3.45 Å R-free 0.218
7M0Z Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP and CH5126766 Deposited 2021-03-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Tris 8.5, 200 mM Lithium Sulfate and 22% PEG 3,350
Resolution 3.12 Å R-free 0.225
7MFD Autoinhibited BRAF:(14-3-3)2:MEK complex with the BRAF RBD resolved Deposited 2021-04-09 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–393（393 aa）
Not recorded ZN ZINC ION × 2 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
7PQV MEK1 IN COMPLEX WITH COMPOUND 7 Deposited 2021-09-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 39–382（344 aa） Fragment：KINASE DOMAIN
Not recorded 80C 8-(2-chloranyl-4-methoxy-phenyl)-7-fluoranyl-1-piperidin-4-yl-imidazo[4,5-c]quinoline × 1 CA CALCIUM ION × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；310 K；The purified protein was used in crystallisation trials employing both, a standard screen with approximately 1200 different conditions, as well as crystallisation conditions identified using literature data. Condi- tions initially obtained have been optimised using standard strategies, systematically varying parameters critically influencing crystallisation, such as temperature, protein concentration, drop ratio, and others. These conditions were also refined by systematically varying pH or precipitant concentrations.
Resolution 2.13 Å R-free 0.287
7XLP MEK1 bound to DS03090629 Deposited 2022-04-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa）
Mutation：S298N, S299K, Y300K FZC (1~{R},3~{S})-3-[[6-[2-chloranyl-4-(4-methylpyrimidin-2-yl)oxy-phenyl]-3-methyl-1~{H}-indazol-4-yl]oxy]cyclohexan-1-amine × 1 DMS DIMETHYL SULFOXIDE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.75；277 K；100 mM Tris (pH 7.75), 200 mM calcium chloride, 2% DMSO, 18-20% PEG 3350
Resolution 2.10 Å R-free 0.246
7XNC MEK1 bound to DS94070624 Deposited 2022-04-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–383（347 aa）
Mutation：S298N, S299K, Y300K GIK ~{N}-[4-[[6-(3-chloranylpyridin-4-yl)-3-methyl-1~{H}-indazol-4-yl]oxy]cyclohexyl]ethanamide × 1 DMS DIMETHYL SULFOXIDE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.75；277 K；100 mM Tris (pH 7.75), 200 mM calcium chloride, 2% DMSO, 18-20% PEG 3350
Resolution 2.10 Å R-free 0.251
8CHF cryo-EM Structure of Craf:14-3-3:Mek1 Deposited 2023-02-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain E 1–393（393 aa）
Chain F 1–393（393 aa）
Not recorded 29L 2-{4-[(1E)-1-(hydroxyimino)-2,3-dihydro-1H-inden-5-yl]-3-(pyridin-4-yl)-1H-pyrazol-1-yl}ethanol × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 4.25 Å
8DGS Cryo-EM structure of a RAS/RAF complex (state 1) Deposited 2022-06-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain B 1–392（392 aa）
Not recorded AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 ZN ZINC ION × 2 MG MAGNESIUM ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.30 Å
8DGT Cryo-EM structure of a RAS/RAF complex (state 2) Deposited 2022-06-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain B 1–392（392 aa）
Not recorded AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 ZN ZINC ION × 2 MG MAGNESIUM ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
8YP4 Structure of MAP2K1 complexed with 5Z7-oxozeaenol Deposited 2024-03-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 34–386（353 aa）
Mutation：T286A, T292A, S298A WNT (4~{S},9~{S},10~{S},12~{E})-16-methoxy-4-methyl-9,10,18-tris(oxidanyl)-3-oxabicyclo[12.4.0]octadeca-1(18),12,14,16-tetraene-2,8-dione × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；8% Tacsimete pH 5.0, 19.5% PEG 3350
Resolution 2.35 Å R-free 0.284
8YP4 Structure of MAP2K1 complexed with 5Z7-oxozeaenol Deposited 2024-03-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 34–386（353 aa）
Mutation：T286A, T292A, S298A WNT (4~{S},9~{S},10~{S},12~{E})-16-methoxy-4-methyl-9,10,18-tris(oxidanyl)-3-oxabicyclo[12.4.0]octadeca-1(18),12,14,16-tetraene-2,8-dione × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；8% Tacsimete pH 5.0, 19.5% PEG 3350
Resolution 2.35 Å R-free 0.284
9AXA CryoEM structure of activated CRAF/MEK/14-3-3 complex with NST-628 Deposited 2024-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 1–393（393 aa）
Chain D 1–393（393 aa）
Mutation：S218A S222A Mutation：S218A S222A A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.36 Å
9AXC Activated CRAF/MEK heterotetramer from focused refinement of CRAF/MEK/14-3-3 complex Deposited 2024-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–393（393 aa）
Chain D 1–393（393 aa）
Mutation：S218A S222A Mutation：S218A S222A A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.16 Å
9AXH Crystal structure of KSR1/MEK1 complex heterotetramer with NST-628 Deposited 2024-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Chain B 37–263（227 aa）
Chain B 308–383（76 aa）
Not recorded A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M SPG buffer pH 7.0, 25% w/v PEG 1500
Resolution 2.81 Å R-free 0.253
9AXM Crystal structure of ARAF/MEK1 complex with NST-628 and a RAF dimer Deposited 2024-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Chain C 37–263（227 aa）
Chain C 308–383（76 aa）
Mutation：S218A S222A Mutation：S218A S222A Mutation：S218A S222A Mutation：S218A S222A A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；291 K；0.1M tri-sodium citrate pH 5.6, 20% 2-propanol, 20% PEG 4000
Resolution 2.42 Å R-free 0.301
9AXX Crystal structure of BRAF/MEK1 complex with NST-628 and an active RAF dimer Deposited 2024-03-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 37–263（227 aa）
Chain A 308–383（76 aa）
Chain C 37–263（227 aa）
Chain C 308–383（76 aa）
Mutation：S218A S222A Mutation：S218A S222A Mutation：S218A S222A Mutation：S218A S222A A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 2 EDO 1,2-ETHANEDIOL × 11 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；0.24 M di-ammonium hydrogen phosphate pH 8.0, 20% w/v PEG 3350
Resolution 2.07 Å R-free 0.248
9AXY Crystal structure of BRAF/MEK complex with NST-628 and inactive RAF Deposited 2024-03-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；0.2 M Lithium chloride, 0.1 M TRIS pH 8, 20% w/v PEG 8000
Resolution 3.60 Å R-free 0.237
9AY7 Crystal structure of CRAF/MEK1 complex with NST-628 and inactive RAF Deposited 2024-03-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A S222A ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 NI NICKEL (II) ION × 1 ACT ACETATE ION × 5 EDO 1,2-ETHANEDIOL × 1 A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；0.2M sodium acetate pH 8.0, 20% w/v PEG 3350
Resolution 2.41 Å R-free 0.236
9AYA Crystal structure of CRAF/MEK complex with NST-628 and active RAF dimer Deposited 2024-03-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 37–263（227 aa）
Chain B 308–383（76 aa）
Chain D 37–263（227 aa）
Chain D 308–383（76 aa）
Mutation：S218A S222A Mutation：S218A S222A Mutation：S218A S222A Mutation：S218A S222A A1AHE N-[3-fluoro-4-({7-[(3-fluoropyridin-2-yl)oxy]-4-methyl-2-oxo-2H-1-benzopyran-3-yl}methyl)pyridin-2-yl]-N'-methylsulfuric diamide × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.2M magnesium chloride, 0.1M tris pH 7.0, 10% w/v PEG 8000
Resolution 2.59 Å R-free 0.257
9ECU Crystal structure of the inactive BRAF/MEK1 complex bound to IK-595 Deposited 2024-11-15 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 4 A1BIS 4-[2-chloro-3-(methylsulfamamido)phenoxy]-N-cyclopropyl-2-(2-fluoro-4-iodoanilino)-1,5-dimethyl-6-oxo-1,6-dihydropyridine-3-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；0.2 M Ammonium Sulfate, 0.1 M Tris pH 8.5, 25% w/v PEG 3350
Resolution 3.46 Å R-free 0.237
9MMP Cryo-EM structure of CRAF/MEK1/14-3-3 complex (autoinhibited conformation) Deposited 2024-12-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–393（393 aa）
Mutation：S218A, S222A AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 ZN ZINC ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50 mM Tris pH 7.5, 150 mM NaCl, 2 mM MgCl2, 0.5 mM TCEP, 2 uM ATPgS, 1 uM GDC0623
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9MMQ Cryo-EM structure of CRAF/MEK1 complex (kinase domain) Deposited 2024-12-20 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50 mM Tris pH 7.5, 150 mM NaCl, 2 mM MgCl2, 0.5 mM TCEP, 2 uM ATPgS, 1 uM GDC0623
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9MMR Cryo-EM structure of CRAF/MEK1/14-3-3 complex (open monomer conformation, CRAF Y340D/Y341D mutant) Deposited 2024-12-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–393（393 aa）
Mutation：S218A, S222A AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50 mM Tris pH 7.5, 150 mM NaCl, 2 mM MgCl2, 0.5 mM TCEP, 2 uM ATPgS, 1 uM GDC0623
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
9MMS Cryo-EM structure of CRAF/MEK1 complex (kinase domain, CRAF Y340D/Y341D mutant) Deposited 2024-12-20 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 LCJ 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)imidazo[1,5-a]pyridine-6-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50 mM Tris pH 7.5, 150 mM NaCl, 2 mM MgCl2, 0.5 mM TCEP, 2 uM ATPgS, 1 uM GDC0623
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9O0U Crystal structure of CRAF/MEK1 complex with PLX4720 and CH5126766 Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 2.91 Å R-free 0.264
9O0U Crystal structure of CRAF/MEK1 complex with PLX4720 and CH5126766 Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 2.91 Å R-free 0.264
9O0U Crystal structure of CRAF/MEK1 complex with PLX4720 and CH5126766 Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 2.91 Å R-free 0.264
9O0U Crystal structure of CRAF/MEK1 complex with PLX4720 and CH5126766 Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 2.91 Å R-free 0.264
9O0V Crystal structure of CRAF/MEK1 complex with PLX4720, CH5126766, and AMPPNP Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 3.50 Å R-free 0.254
9O0V Crystal structure of CRAF/MEK1 complex with PLX4720, CH5126766, and AMPPNP Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 3.50 Å R-free 0.254
9O0V Crystal structure of CRAF/MEK1 complex with PLX4720, CH5126766, and AMPPNP Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 3.50 Å R-free 0.254
9O0V Crystal structure of CRAF/MEK1 complex with PLX4720, CH5126766, and AMPPNP Deposited 2025-04-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 1–393（393 aa）
Mutation：S218A, S222A 324 N-{3-[(5-chloro-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]-2,4-difluorophenyl}propane-1-sulfonamide × 1 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；18% PEG 3350, 0.1 M Sodium citrate pH 5.6, 4% Tacsimate pH 5
Resolution 3.50 Å R-free 0.254
9O2Z Autoinhibited BRAF:(14-3-3)2:MEK complex from Insect cells Deposited 2025-04-04 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–393（393 aa）
Not recorded ZN ZINC ION × 2 CHU N-(3-fluoro-4-{[4-methyl-2-oxo-7-(pyrimidin-2-yloxy)-2H-chromen-3-yl]methyl}pyridin-2-yl)-N'-methylsulfuric diamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.83 Å
9TYG Structure of the MAP2K MEK1 in an inactive conformation in complex with its substrate MAPK ERK2 Deposited 2026-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–2（2 aa）
Chain A 12–393（382 aa）
Mutation：residue 3-11 replaced with 15 residues GRA24 KIM,Ser218Asp,Ser222Asp Mutation：residue 3-11 replaced with 15 residues GRA24 KIM,Ser218Asp,Ser222Asp ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9TYH Structure of the MAP2K MEK1 in an active conformation in complex with its substrate MAPK ERK2 Deposited 2026-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–2（2 aa）
Chain A 12–393（382 aa）
Mutation：residue 3-11 replaced with GRA24 KIM (15 residues),Ser218Asp,Ser222Asp Mutation：residue 3-11 replaced with GRA24 KIM (15 residues),Ser218Asp,Ser222Asp ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9TYI Structure of the MAP2K MEK1 without bound nucleotide in complex with its substrate MAPK ERK2 Deposited 2026-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–2（2 aa）
Chain A 12–393（382 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9UUR The complex of human pMEK1 and uERK1 (ANP) Deposited 2025-05-08 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–393（393 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.36 Å
9UUX The complex of human pMEK1 and ERK1 pT202 (ANP) Deposited 2025-05-08 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–393（393 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.12 Å
9UW3 The complex of human pMEK1 and ERK1 pY204 (ANP) Deposited 2025-05-12 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–393（393 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.36 Å
9UW4 The complex of human pMEK1 and uERK1 (ANP)(from pY204ERK1) Deposited 2025-05-12 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–393（393 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å

92 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MP2K1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 26–384； UniProt 35–393

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7umb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7umb
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id7umb
Deposition date deposition_date2022-04-06
Structure title titleNanoBRET tracer Tram-bo bound to a KSR2-MEK1 complex
Keywords keywordsTracer, kinase, complex, MEK1, KSR2, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier27.97 Å
Radius of gyration Rg (electron density) rg_electron27.20 Å
Forward intensity I(0) i074863000.00
Molecular weight molecular_weight68202.0 kDa
Excluded volume excluded_volume85646 ų
Envelope volume envelope_volume107920 ų
Hydration-shell volume shell_volume33147 ų
Envelope diameter envelope_diameter92.3 Å
Shell Rg shell_rg34.62 Å
Envelope Rg envelope_rg27.08 Å
Shape Rg shape_rg27.21 Å
Total Rg total_rg27.96 Å
Total atoms total_atoms4781
Residues n_residues580
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax86.8 Å
Rg (real space) rg_real27.94 Å
Rg uncertainty (real space) rg_real_error0.54 Å
I(0) (real space) i0_real7.4860e+07
I(0) uncertainty (real space) i0_real_error1.1050e+06
Rg (reciprocal space) rg_reciprocal27.95 Å
I(0) (reciprocal space) i0_reciprocal74860000.0000
Solution quality estimate total_estimate0.9048
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4 Å
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.2850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37840000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.923
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

▶

8. Citations (1)

▶

9. Files and Curves (10)