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9mms

Cryo-EM structure of CRAF/MEK1 complex (kinase domain, CRAF Y340D/Y341D mutant)

Method: ELECTRON MICROSCOPY Dmax: 80.2 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

RAF proto-oncogene serine/threonine-protein kinase

Homo sapiens

UniProt P04049

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 A； UniProt 1–648 Mutation：Q156R, Y340D, Y341D, D587E Dual specificity mitogen-activated protein kinase kinase 1 × 1 （Q02750） 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

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 9MMS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C1Y CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD). Deposited 1999-07-22 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 55–131（77 aa） Fragment：RAFRBD, RESIDUES 51-131
Not recorded MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；300 K；mmePeg5000, magnesium chloride, calcium chloride, ammonium sulphate., pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 1.90 Å R-free 0.257
1FAQ RAF-1 CYSTEINE RICH DOMAIN, NMR, 27 STRUCTURES Deposited 1996-09-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 136–187（52 aa） Fragment：CYSTEINE-RICH DOMAIN
Not recorded ZN ZINC ION × 2 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1FAR RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-09-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 136–187（52 aa） Fragment：CYSTEINE-RICH DOMAIN
Not recorded ZN ZINC ION × 2 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1GUA HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131 Deposited 1996-06-18 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 51–131（81 aa） Fragment：RESIDUES 51-131
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1RFA NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1 Deposited 1995-04-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 55–132（78 aa） Fragment：RAS BINDING DOMAIN, RESIDUES 55 - 132 WITH AN ADDITIONAL ALA AT THE N-TERMINUS
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
3CU8 Impaired binding of 14-3-3 to Raf1 is linked to Noonan and LEOPARD syndrome Deposited 2008-04-16 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 P 256–264（9 aa） Fragment：Phosphorylated cRaf1 peptide
Chain Q 256–264（9 aa） Fragment：Phosphorylated cRaf1 peptide
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 2 PPI PROPANOIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M (Sodium propionate, sodium cacodylate, BIS-TRIS propane), 27% PEG 1500, 2mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.259
3IQJ Crystal Structure of human 14-3-3 sigma in Complex with Raf1 peptide (10mer) Deposited 2009-08-20 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 P 255–264（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes/NaOH ph 7.5, 0.2M CaCl2, 28% PEG 400, 5% glycerol, 2mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.15 Å R-free 0.153
3IQU Crystal Structure of human 14-3-3 sigma in Complex with Raf1 peptide (6mer) Deposited 2009-08-21 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 P 255–260（6 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes/NaOH ph 7.5, 0.2M CaCl2, 28% PEG 400, 5% glycerol, 2mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.05 Å R-free 0.151
3IQV Crystal Structure of human 14-3-3 sigma in Complex with Raf1 peptide (6mer) and stabilisator Fusicoccin Deposited 2009-08-21 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 P 255–260（6 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) FSC FUSICOCCIN × 2 CL CHLORIDE ION × 4 MG MAGNESIUM ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；20mM Hepes/NaOH pH 7.5, 2mM MgCl2 and 2 mM DTT, set up for crystallization in 0.1 M Hepes/NaOH ph 7.5, 0.2 M CaCl2, 28% PEG 400, 5% glycerol, 2mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.20 Å R-free 0.153
3KUC Complex of Rap1A(E30D/K31E)GDP with RafRBD(A85K/N71R) Deposited 2009-11-27 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 51–131（81 aa） Fragment：UNP residues 51-131
Mutation：A85K, N71R GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；20-25% PEG 8000, 100 mM Tris or HEPES pH 7.2-7.6, 10-200 mM Ca Acetate or 100 mM Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.92 Å R-free 0.209
3KUD Complex of Ras-GDP with RafRBD(A85K) Deposited 2009-11-27 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 51–131（81 aa） Fragment：UNP residues 51-131
Mutation：A85K GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；1.3M Na-Malonat pH 6.0, 100 mM MES pH 6.1, 4% Betaine, 2% Sarcosine, 2% N,N-dimethylglycine, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.15 Å R-free 0.264
3NKX Impaired binding of 14-3-3 to Raf1 is linked to Noonan and LEOPARD syndrome Deposited 2010-06-21 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 P 255–264（10 aa） Fragment：phosphorylated C-Raf peptide, UNP residues 255-264
Chain Q 255–264（10 aa） Fragment：phosphorylated C-Raf peptide, UNP residues 255-264
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) PPI PROPANOIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M (Sodium propionate, sodium cacodylate, BIS-TRIS propane), 27% PEG 1500, 2mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.40 Å R-free 0.247
3O8I Structure of 14-3-3 isoform sigma in complex with a C-Raf1 peptide and a stabilizing small molecule fragment Deposited 2010-08-03 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 255–264（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) M1T 6,6-dihydroxy-1-methoxyhexan-2-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277.15 K；0.095M HEPES Na, 26.6%(v/v) PEG400, 0.19M CaCl2, 5%(v/v) Glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K
Resolution 2.00 Å R-free 0.239
3OMV Crystal structure of c-raf (raf-1) Deposited 2010-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 323–618（296 aa） Fragment：C-RAF kinase domain, UNP residues 323-618
Chain B 323–618（296 aa） Fragment：C-RAF kinase domain, UNP residues 323-618
Not recorded SM5 (1E)-5-(1-piperidin-4-yl-3-pyridin-4-yl-1H-pyrazol-4-yl)-2,3-dihydro-1H-inden-1-one oxime × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；285 K；12% PEG 8K, 100 MM TRIS PH 8.0, 10% TACSIMATE, VAPOR DIFFUSION, HANGING DROP, temperature 285K
Resolution 4.00 Å R-free 0.364
4FJ3 14-3-3 isoform zeta in complex with a diphoyphorylated C-RAF peptide Deposited 2012-06-11 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 × 3 PDB declaration: trimeric
Chain P 229–264（36 aa） Fragment：UNP residues 229-264
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；0.1 M Na-acetate pH 7.0, 0.8 M NaH2PO4 and 1.2 M K2HPO4 , VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.95 Å R-free 0.208
4G0N Crystal Structure of wt H-Ras-GppNHp bound to the RBD of Raf Kinase Deposited 2012-07-09 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 54–131（78 aa） Fragment：UNP residues 54-131
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 CA CALCIUM ION × 2 MG MAGNESIUM ION × 1 ACT ACETATE ION × 1 DTU (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.8；291 K；Protein solution: 10 - 16 mg/mL, 50 mM HEPES, pH 7.2, 50 mM NaCl, 10mM MgCl2 5% Glycerol, 1mM DTE, 10 M ZnCl2 Reservoir solution:200mM calcium acetate, 100mM sodium cacodylate pH 6.5, 18% PEG 8000. Drop: 1uL protein, 1uL reservoir, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.45 Å R-free 0.229
4G3X Crystal Structure of Q61L H-Ras-GppNHp bound to the RBD of Raf Kinase Deposited 2012-07-15 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 55–131（77 aa） Fragment：UNP residues 55-131
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；291 K；Protein solution: 10 - 18 mg/mL, 50 mM HEPES, pH 7.2, 50 mM NaCl, 10mM MgCl2 5% Glycerol, 1mM DTE, 10 M ZnCl2 Reservoir solution:200mM calcium acetate, 100mM sodium cacodylate pH 6.5, 18% PEG 8000. Drop: 3uL protein, 3uL reservoir , VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.25 Å R-free 0.271
4IEA 14-3-3 isoform sigma in complex with a phosphorylated C-RAF peptide Deposited 2012-12-13 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 P 618–625（8 aa） Fragment：UNP residues 618-625
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；95 mM Na-HEPES pH 7.4, 25.6 % PEG 400, 190 mM CaCl2, 5 % Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.70 Å R-free 0.208
4IHL Human 14-3-3 isoform zeta in complex with a diphoyphorylated C-RAF peptide and Cotylenin A Deposited 2012-12-19 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 × 3 PDB declaration: trimeric
Chain P 229–264（36 aa） Fragment：UNP residues 229-264
Non-standard monomer：Yes (specific site not provided by mmCIF) K POTASSIUM ION × 2 1F5 (1R,3aS,4R,5R,6R,9aR,10E)-6-({(1S,2R,4S,5R,6R,8S,9S)-5-hydroxy-2-(methoxymethyl)-9-methyl-9-[(2S)-oxiran-2-yl]-3,7,10,1 1-tetraoxatricyclo[6.2.1.0~1,6~]undec-4-yl}oxy)-1-(methoxymethyl)-4,9a-dimethyl-7-(propan-2-yl)-1,2,3,3a,4,5,6,8,9,9a-de cahydrodicyclopenta[a,d][8]annulene-1,5-diol × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；0.1 M NA-ACETATE PH 7.0, 0.8 M NAH2PO4 AND 1.2 M K2HPO4, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.20 Å R-free 0.243
6NTC Crystal Structure of G12V HRas-GppNHp bound in complex with the engineered RBD variant 1 of CRAF Kinase protein Deposited 2019-01-28 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 55–131（77 aa）
Mutation：F61L, K65Q, Q66E, R67W, N71K, C81S, V88R, R89H, C95S, C96S GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 GOL GLYCEROL × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293.15 K；30% PEG4000, 200mM NH4SO4, 100mM Na CaCo pH 6.5
Resolution 2.90 Å R-free 0.278
6NTD Crystal Structure of G12V HRas-GppNHp bound in complex with the engineered RBD variant 12 of CRAF Kinase protein Deposited 2019-01-28 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 55–131（77 aa）
Mutation：F61L, K65H, Q66E, N71K, C81S, V88R, R89H, C95S, C96S MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；30% PEG4000, 200mM NH4SO4, 100mM Na Citrate
Resolution 3.15 Å R-free 0.287
6PTS NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state A) Deposited 2019-07-16 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 D 56–187（132 aa） Fragment：RBD-CRD (UNP residues 56-187)
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C KRAS, 0.2 mM U-12C, 14N, 1H RBD-CRD, 0.4 mM U-12C, 14N, 1H MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 0.4 mM U-12C, 14N, 1H MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM U-15N; Ile C-delta-13C, Met methyl-13C KRAS, 0.5 mM Leu C-delta-13C, Val C-gamma-13C, RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-99% 15N]; [U-13C]; RBD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM [U-99% 15N]; [U-13C]; CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PTW NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state B) Deposited 2019-07-16 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 D 56–187（132 aa） Fragment：RBD-CRD (UNP residues 56-187)
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N; U-2H] KRAS, 0.2 mM [U-12C; U-14N; U-1H] RBD-CRD, 0.4 mM [U-12C; U-14N; U-1H] MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [U-12C; U-14N; U-1H] KRAS, 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N; U-2H] RBD-CRD, 0.4 mM [U-12C; U-14N; U-1H] MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N] RBD-CRD, 0.2 mM [U-12C; U-14N; U-1H] KRAS Q43C, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N] RBD-CRD, 0.2 mM [U-12C; U-14N; U-1H] KRAS N-term C, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-15N; Ile C-delta-13C; Met methyl-13C] KRAS, 0.5 mM [Leu C-delta-13C; Val C-gamma-13C] RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-13C; U-15N] RBD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-13C; U-15N] CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6VJJ Crystal Structure of wild-type KRAS4b (GMPPNP-bound) in complex with RAS-binding domain (RBD) of RAF1/CRAF Deposited 2020-01-16 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 52–131（80 aa）
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 CL CHLORIDE ION × 3 EDO 1,2-ETHANEDIOL × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.09M Halogens, 0.1M Imidazole.MES pH 6.5, 37.5% MPD, PEG 1000 and PEG 3350
Resolution 1.40 Å R-free 0.195
6XGU Crystal Structure of KRAS-Q61R (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF Deposited 2020-06-18 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 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 3 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.8；293 K；100 mM Tris 7.8, 200 mM KBr, 200 mM KSCN, 3% PGA, 0.35 mM D-myo-phosphatidylinositol 3,4,5-triphosphate
Resolution 2.70 Å R-free 0.236
6XGV Crystal Structure of KRAS-G13D (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF Deposited 2020-06-18 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 52–188（137 aa）
Mutation：Modified Cys95 Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 3 GOL GLYCEROL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM sodium cacodylate pH 6.5, 700 mM sodium acetate, 0.35 mM D-myo-phosphatidylinositol 3,4,5-triphosphate
Resolution 2.11 Å R-free 0.204
6XHA Crystal Structure of KRAS-G12V (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF Deposited 2020-06-18 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 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 GOL GLYCEROL × 4 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM sodium cacodylate pH 6.5, 200 mM MgCl2, 8% PGA, 0.35 mM D-myo-phosphatidylinositol 3,4,5-triphosphate
Resolution 2.87 Å R-free 0.269
6XHB Crystal Structure of wild-type KRAS (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF (crystal form II) Deposited 2020-06-18 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 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 3 GOL GLYCEROL × 2 IPA ISOPROPYL ALCOHOL × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；100 mM sodium cacodylate pH 6.5, 200 mM sodium citrate, 15% 2-propanol, 0.25% (w/v) n-octyl-beta-D-glucoside, 0.35 mM D-myo-phosphatidylinositol 3,4,5-triphosphate, and 0.25% (w/v) n-dodecyl-beta-D-maltoside
Resolution 2.50 Å R-free 0.221
6XI7 Crystal Structure of wild-type KRAS (GMPPNP-bound) in complex with RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF1/CRAF (crystal form I) Deposited 2020-06-19 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 52–188（137 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 2 CL CHLORIDE ION × 5 ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.3；293 K；2218.18 mM AMSO4, 6.5% (w/v) PEG 400, pH 5.3
Resolution 1.95 Å R-free 0.232
7JHP Crystal structure of HRas in complex with the Ras-binding and cysteine-rich domains of CRaf-kinase Deposited 2020-07-21 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 C 55–187（133 aa） Fragment：UNP residues 55-187
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 17% w/v PEG10000
Resolution 2.77 Å R-free 0.264
7Z37 Structure of the RAF1-HSP90-CDC37 complex (RHC-II) Deposited 2022-03-01 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 CP1 1–648（648 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds before plunging
Resolution 3.67 Å
7Z38 Structure of the RAF1-HSP90-CDC37 complex (RHC-I) Deposited 2022-03-01 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 C 1–648（648 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；blot for 3 seconds before plunging
Resolution 3.16 Å
8A68 Small molecule stabilizer (compound 5) for C-RAF(pS259) and 14-3-3 Deposited 2022-06-16 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 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 6 L7U ~{N}-[2-[2-(dimethylamino)ethyldisulfanyl]ethyl]-1-[(2~{R})-2-(6-methoxynaphthalen-2-yl)propanoyl]piperidine-4-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH 7.5, 0.19 M CaCl2, 5% glycerol, 28% PEG 400
Resolution 1.60 Å R-free 0.179
8A6F Small molecule stabilizer (compound 8) for C-RAF and 14-3-3 Deposited 2022-06-17 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 P 255–264（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 O56 1-[4-[4-chloranyl-3-(trifluoromethyl)phenyl]-4-oxidanyl-piperidin-1-yl]-3-[2-(dimethylamino)ethyldisulfanyl]propan-1-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH 7.5, 0.19 M CaCl2, 26% (v/v) PEG 400 and 5% (v/v) glycerol
Resolution 1.60 Å R-free 0.181
8A6H Small molecule stabilizer (compound 7) for C-RAF and 14-3-3 Deposited 2022-06-17 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 P 255–264（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 L6L 3-[2-(dimethylamino)ethyldisulfanyl]-1-[4-oxidanyl-4-[3-(trifluoromethyl)phenyl]piperidin-1-yl]propan-1-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH 7.7, 0.19 M CaCl2, 24 % (v/v) PEG 400 and 5% (v/v) glycerol)
Resolution 1.60 Å R-free 0.174
8ATR Small molecular stabilizer for C-RAF (pS259) and 14-3-3 (1075297) Deposited 2022-08-24 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 P 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 O6L 2-chloranyl-~{N}-[[1-[1-(4-chloranylphenoxy)cyclopentyl]carbonylpiperidin-4-yl]methyl]ethanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES (pH 7.1), PEG400 (24% (v/v)), 0.19 M CaCl2 and 5% (v/v) Glycerol
Resolution 1.70 Å R-free 0.211
8ATS Small molecular stabilizer for C-RAF (pS259) and 14-3-3 (1075306) Deposited 2022-08-24 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 P 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 O5I 2-chloranyl-~{N}-[[1-[1-[(4-chlorophenyl)amino]cyclopentyl]carbonylpiperidin-4-yl]methyl]ethanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES (pH 7.1), PEG400 (24% (v/v)), 0.19 M CaCl2 and 5% (v/v) Glycerol
Resolution 1.40 Å R-free 0.171
8AV0 small molecule stabilizer (compound 1) for C-RAF pS259 and 14-3-3 Deposited 2022-08-26 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 P 256–264（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 O6C 1-[2-(4-chloranylphenoxy)-2-methyl-propanoyl]-~{N}-[2-[2-(dimethylamino)ethyldisulfanyl]ethyl]piperidine-4-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES (pH 7.1), PEG400 (24% (v/v)), 0.19 M CaCl2 and 5% (v/v) Glycerol
Resolution 1.50 Å R-free 0.180
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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–648（648 aa）
Chain B 1–648（648 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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
8CPD Cryo-EM structure of CRaf dimer with 14:3:3 Deposited 2023-03-02 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 1–648（648 aa）
Chain B 1–648（648 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.46 Å
8EPW Crystal Structure of KRAS4b-G13D (GMPPNP-bound) in complex with RAS-binding domain (RBD) of RAF1/CRAF Deposited 2022-10-06 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 52–131（80 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.15 M potassium bromide, 30% PEG 2000 MME
Resolution 2.00 Å R-free 0.253
8GAE Hsp90 provides platform for CRaf dephosphorylation by PP5 Deposited 2023-02-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain D 404–610（207 aa）
Not recorded K POTASSIUM ION × 2 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE
Resolution 3.30 Å
8GFT Hsp90 provides platform for CRaf dephosphorylation by PP5 Deposited 2023-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain D 336–618（283 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；3uL OF SAMPLE, 10C, 100% HUMIDITY, 30S WAIT TIME, 3S BLOT TIME, -2 BLOT FORCE
Resolution 3.80 Å
8JNA CRAF ras-binding domain chimera, apo form Deposited 2023-06-06 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 Monomer；Protein × 1 PDB declaration: monomeric
Chain B 50–101（52 aa）
Chain B 114–141（28 aa）
Mutation：K65S, F99Y, S120W, D129E Mutation：K65S, F99Y, S120W, D129E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；1.0M tri-sodium citrate, 0.1M imidazole, pH 8.0
Resolution 1.70 Å R-free 0.272
8JNB CRAF ras-binding domain chimera, ligand complex Deposited 2023-06-06 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 Monomer；Protein × 1 PDB declaration: monomeric
Chain B 50–101（52 aa）
Chain B 114–141（28 aa）
Mutation：K65S, F99Y, S120W, D129E Mutation：K65S, F99Y, S120W, D129E USX 2-[4-[[(2S)-1-ethanoyl-3-oxidanylidene-2H-indol-2-yl]methyl]-2-methoxy-phenoxy]ethanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293 K；0.5M ammonium sulfate, 1.0M lithium sulfate, 0.1M sodium citrate, pH 5.6
Resolution 1.62 Å R-free 0.242
8JOF solution-structure of Ras Binding Domain (RBD) in C-RAF Deposited 2023-06-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 51–131（81 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 85；Pressure ambient
NMR sample composition 0.3 mM [U-100% 13C; U-100% 15N] Serine/threonine-protein Kinase C-RAF, 25 mM sodium phosphate, 50 mM sodium chloride, 10 mM magnesium dichloride, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8JOG solution structure of Ras Binding Domein (RBD) in C-RAF with negative allosteric modulator. Deposited 2023-06-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 51–131（81 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 85；Pressure ambient
NMR sample composition 0.3 mM [U-100% 13C; U-100% 15N] Serin/threonine protein kinase C-RAF, 25 mM sodium phosphate, 50 mM sodium chloride, 10 mM magnesium dichloride, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8S42 Ternary structure of 14-3-3s, C-RAF phosphopeptide (pS259) and compound 80 (1124898) Deposited 2024-02-21 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 P 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 A1H5F 2-chloranyl-1-[8-[3-fluoranyl-4-(trifluoromethyl)phenyl]sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.70 Å R-free 0.194
8T74 Crystal structure of KRAS4a (GMPPNP) in complex with RAF1 (RBD) Deposited 2023-06-19 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 52–131（80 aa）
Not recorded MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.15 M DL-malic acid (pH 7.0), 20% PEG 3350
Resolution 1.65 Å R-free 0.196
8T75 Crystal Structure of KRAS4a (GMPPNP) in complex with RAF1 (RBD-CRD) Deposited 2023-06-19 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 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M sodium acetate (pH 4.6), 2 M sodium formate
Resolution 2.65 Å R-free 0.219
8T75 Crystal Structure of KRAS4a (GMPPNP) in complex with RAF1 (RBD-CRD) Deposited 2023-06-19 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M sodium acetate (pH 4.6), 2 M sodium formate
Resolution 2.65 Å R-free 0.219
8T75 Crystal Structure of KRAS4a (GMPPNP) in complex with RAF1 (RBD-CRD) Deposited 2023-06-19 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M sodium acetate (pH 4.6), 2 M sodium formate
Resolution 2.65 Å R-free 0.219
8T75 Crystal Structure of KRAS4a (GMPPNP) in complex with RAF1 (RBD-CRD) Deposited 2023-06-19 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 52–188（137 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M sodium acetate (pH 4.6), 2 M sodium formate
Resolution 2.65 Å R-free 0.219
8U1L Cryo-EM structure of the RAF1-HSP90-CDC37 complex in the closed state Deposited 2023-09-01 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 C 2–648（647 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.3
cryo-EM vitrification conditions Cryogen ETHANE；Grids were blotted for 4.5 seconds before plunging
Resolution 3.70 Å
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 conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 306–648（343 aa）
Chain C 306–648（343 aa）
Mutation：Y340D Y341D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y340D Y341D Non-standard monomer：Yes (specific site not provided by mmCIF) 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 conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 306–648（343 aa）
Chain C 306–648（343 aa）
Mutation：Y340D Y341D Mutation：Y340D Y341D 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
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 method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 337–615（279 aa）
Mutation：Y340D Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 337–615（279 aa）
Chain C 337–615（279 aa）
Mutation：Y340D Y341D Mutation：Y340D Y341D 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
9EW1 Ternary structure of 14-3-3s, CRAF phosphopeptide (pS259) and compound 79 (1124379). Deposited 2024-04-03 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 P 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 WQT 2-chloranyl-1-[8-(4-iodophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.40 Å R-free 0.168
9EW3 Ternary structure of 14-3-3s, C-RAF phosphopeptide 12-mer (pS259) and compound 78 (1084378) Deposited 2024-04-03 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 P 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 WQN 1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.40 Å R-free 0.229
9EW4 Ternary structure of 14-3-3s, C-RAF phosphopeptide 12mer (pS259) and compound 86 (1124384) Deposited 2024-04-03 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 P 255–263（9 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 8 WQ9 1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.60 Å R-free 0.211
9EW5 Ternary structure of 14-3-3s, C-RAF phosphopeptide (pS259) 12mer and compound 23 (1083848) Deposited 2024-04-03 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 C 255–265（11 aa）
Chain F 255–265（11 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) WQI 2-chloranyl-~{N}-[[1-(4-iodophenyl)sulfonylpiperidin-4-yl]methyl]ethanamide × 2 CA CALCIUM ION × 3 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.50 Å R-free 0.216
9EW7 Binary structure of 14-3-3s and CRAF phosphopeptide (pS259) Deposited 2024-04-03 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 P 255–264（10 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.80 Å R-free 0.193
9MMP Cryo-EM structure of CRAF/MEK1/14-3-3 complex (autoinhibited conformation) Deposited 2024-12-20 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–648（648 aa）
Mutation：Q156R, D587E Non-standard monomer：Yes (specific site not provided by mmCIF) 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 mutation/modification Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–648（648 aa）
Mutation：Q156R, D587E 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 mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–648（648 aa）
Mutation：Q156R, Y340D, Y341D, D587E Non-standard monomer：Yes (specific site not provided by mmCIF) 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
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 method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 337–615（279 aa）
Mutation：Y340D, Y341D 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 method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 337–615（279 aa）
Mutation：Y340D, Y341D 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
9S2I Ternary structure of 14-3-3, CRAF R256S NS mutant phosphopeptide (pS259), and compound 78 (1124378) Deposited 2025-07-21 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 P 255–265（11 aa）
Mutation：R256S Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 WQN 1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.67 Å R-free 0.201
9S2J Ternary structure of 14-3-3s, CRAF S257L NS mutant phosphopeptide (pS259) and compound 78 (1084378) Deposited 2025-07-21 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 P 255–265（11 aa）
Mutation：S257L Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 WQN 1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.50 Å R-free 0.203
9S2K Ternary structure of 14-3-3s, CRAF V263A NS mutant phosphopeptide (pS259), and compound 78 (1124378) Deposited 2025-07-21 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 P 255–265（11 aa）
Mutation：V263A Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 6 WQN 1-[8-(4-bromophenyl)sulfonyl-5-oxa-2,8-diazaspiro[3.5]nonan-2-yl]-2-chloranyl-ethanone × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 2.15 Å R-free 0.233
9S2L Ternary structure of 14-3-3s, CRAF R256S NS mutant phosphopeptide (pS259), and compound 23 (1083848) Deposited 2025-07-21 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 H 255–265（11 aa）
Chain S 255–265（11 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) WQI 2-chloranyl-~{N}-[[1-(4-iodophenyl)sulfonylpiperidin-4-yl]methyl]ethanamide × 2 MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.85 Å R-free 0.223
9S2M Ternary structure of 14-3-3s, CRAF S257L NS mutant phosphopeptide (pS259), and compound 23 (1083848) Deposited 2025-07-21 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 H 255–265（11 aa）
Chain S 255–265（11 aa）
Mutation：S257L Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S257L Non-standard monomer：Yes (specific site not provided by mmCIF) WQI 2-chloranyl-~{N}-[[1-(4-iodophenyl)sulfonylpiperidin-4-yl]methyl]ethanamide × 2 MG MAGNESIUM ION × 5 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 2.00 Å R-free 0.227
9S2N Ternary structure of 14-3-3s, CRAF V263A NS mutant phosphopeptide (pS259), and compound 23 (1083848) Deposited 2025-07-21 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 H 255–264（10 aa）
Chain S 255–264（10 aa）
Mutation：V263A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：V263A Non-standard monomer：Yes (specific site not provided by mmCIF) WQI 2-chloranyl-~{N}-[[1-(4-iodophenyl)sulfonylpiperidin-4-yl]methyl]ethanamide × 2 MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.85 Å R-free 0.239
9S2O Ternary structure of 14-3-3s, CRAF R256S NS mutant phosphopeptide (pS259), and compound 22 (1083853) Deposited 2025-07-21 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 H 255–265（11 aa）
Chain S 255–265（11 aa）
Mutation：R256S Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R256S Non-standard monomer：Yes (specific site not provided by mmCIF) WPN ~{N}-[[1-(4-bromophenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide × 2 MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.80 Å R-free 0.213
9S2P Ternary structure of 14-3-3s, CRAF V263A NS mutant phosphopeptide (pS259), and compound 22 (1083853) Deposited 2025-07-21 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 P 255–265（11 aa）
Mutation：V263A Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 MG MAGNESIUM ION × 4 WPN ~{N}-[[1-(4-bromophenyl)sulfonylpiperidin-4-yl]methyl]-2-chloranyl-ethanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.095 M HEPES pH=7.1-7.7 0.19 M CaCl2 5% glycerol 24-29% PEG400
Resolution 1.50 Å R-free 0.197
9YGS Crystal structure of GMPPNP bound KRAS-Y71H in complex with RBD domain of CRAF(RAF1) Deposited 2025-09-29 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 52–131（80 aa）
Not recorded GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；100 mM Potassium thiocyanate, 30% PEG monomethyl ether 2000.
Resolution 1.68 Å R-free 0.233

74 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAF1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 23–670； UniProt 1–648

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 B； UniProt 1–393 Mutation：S218A, S222A RAF proto-oncogene serine/threonine-protein kinase × 1 （P04049） 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

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 9MMS 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 method 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 oligomeric state Different ligand/ion 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 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 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 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 oligomeric state Different ligand/ion 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 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 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 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 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 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 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 method 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 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 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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
7UMB NanoBRET tracer Tram-bo bound to a KSR2-MEK1 complex Deposited 2022-04-06 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 C 35–393（359 aa）
Not recorded 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
7XLP MEK1 bound to DS03090629 Deposited 2022-04-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 method 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 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 method 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 method 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 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 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 method 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 method 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 method 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 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）
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 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 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 method 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 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）
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 oligomeric state Different ligand/ion 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 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 oligomeric state 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
9O0U Crystal structure of CRAF/MEK1 complex with PLX4720 and CH5126766 Deposited 2025-04-03 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 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 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 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 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 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 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 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 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 mutation/modification Different ligand/ion 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 mutation/modification Different ligand/ion 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 mutation/modification Different ligand/ion 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 mutation/modification Different ligand/ion 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 B； PDBConstruct 23–415； UniProt 1–393

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 9mms

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mms
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mms
Deposition date deposition_date2024-12-20
Structure title titleCryo-EM structure of CRAF/MEK1 complex (kinase domain, CRAF Y340D/Y341D mutant)
Keywords keywordsCRAF-MEK1-14-3-3 complex, MAPK pathway, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.22 Å
Radius of gyration Rg (electron density) rg_electron24.51 Å
Forward intensity I(0) i065078100.00
Molecular weight molecular_weight63046.0 kDa
Excluded volume excluded_volume78932 ų
Envelope volume envelope_volume92452 ų
Hydration-shell volume shell_volume30911 ų
Envelope diameter envelope_diameter83.8 Å
Shell Rg shell_rg32.33 Å
Envelope Rg envelope_rg24.52 Å
Shape Rg shape_rg24.53 Å
Total Rg total_rg25.28 Å
Total atoms total_atoms4410
Residues n_residues546
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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax80.2 Å
Rg (real space) rg_real25.14 Å
Rg uncertainty (real space) rg_real_error0.40 Å
I(0) (real space) i0_real6.5080e+07
I(0) uncertainty (real space) i0_real_error8.0900e+05
Rg (reciprocal space) rg_reciprocal25.16 Å
I(0) (reciprocal space) i0_reciprocal65080000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3 Å
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.3150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20470000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)