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Fluorine in PDB 4ark: Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp:
2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp, PDB code: 4ark was solved by I.V.Hartung, M.Hitchcock, F.Puehler, R.Neuhaus, A.Scholz, S.Hammer, K.Petersen, G.Siemeister, D.Brittain, R.C.Hillig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.80 / 2.60
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 82.411, 82.411, 130.238, 90.00, 90.00, 120.00
R / Rfree (%) 17.205 / 21.135

Other elements in 4ark:

The structure of Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Iodine (I) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp (pdb code 4ark). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp, PDB code: 4ark:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 4ark

Go back to Fluorine Binding Sites List in 4ark
Fluorine binding site 1 out of 2 in the Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1385

b:73.8
occ:1.00
F24 A:M3K1385 0.0 73.8 1.0
C06 A:M3K1385 1.3 74.7 1.0
C01 A:M3K1385 2.3 73.0 1.0
C05 A:M3K1385 2.3 75.7 1.0
N07 A:M3K1385 2.7 70.9 1.0
OD1 A:ASP208 2.9 69.9 1.0
CD A:LYS97 3.2 66.8 1.0
C02 A:M3K1385 3.5 72.7 1.0
C04 A:M3K1385 3.6 75.5 1.0
O16 A:M3K1385 3.6 66.0 1.0
O A:HOH2025 3.7 57.4 1.0
CD1 A:ILE141 3.8 66.9 1.0
CE A:LYS97 3.9 71.8 1.0
C03 A:M3K1385 4.0 73.7 1.0
C08 A:M3K1385 4.1 68.6 1.0
CG A:ASP208 4.1 66.5 1.0
CE A:MET143 4.1 77.9 1.0
SD A:MET143 4.2 71.6 1.0
CG2 A:ILE141 4.2 60.8 1.0
CB A:ILE141 4.3 63.9 1.0
CG A:LYS97 4.5 68.2 1.0
CB A:LYS97 4.5 64.9 1.0
CA A:ASP208 4.5 62.2 1.0
N A:ASP208 4.5 62.2 1.0
C14 A:M3K1385 4.6 68.0 1.0
CG A:MET143 4.7 68.5 1.0
CG1 A:ILE141 4.7 65.0 1.0
C09 A:M3K1385 4.8 68.5 1.0
OD2 A:ASP208 4.9 65.2 1.0
CB A:ASP208 5.0 61.5 1.0

Fluorine binding site 2 out of 2 in 4ark

Go back to Fluorine Binding Sites List in 4ark
Fluorine binding site 2 out of 2 in the Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Catalytic Domain of Human Map Kinase Kinase 1 (MEK1) in Complex with A Small Molecule Inhibitor and Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1385

b:66.5
occ:1.00
F26 A:M3K1385 0.0 66.5 1.0
C12 A:M3K1385 1.3 67.6 1.0
C11 A:M3K1385 2.3 67.0 1.0
C13 A:M3K1385 2.3 67.5 1.0
N A:SER212 2.9 78.6 1.0
N A:VAL211 3.1 73.0 1.0
CG2 A:VAL211 3.4 80.0 1.0
O A:PHE209 3.5 56.3 1.0
C10 A:M3K1385 3.5 68.0 1.0
C08 A:M3K1385 3.6 68.6 1.0
C A:GLY210 3.6 72.2 1.0
CB A:SER212 3.7 83.3 1.0
CA A:GLY210 3.7 65.8 1.0
CA A:SER212 3.8 81.5 1.0
CA A:VAL211 3.8 76.6 1.0
C A:VAL211 3.8 79.6 1.0
O A:SER212 3.9 80.9 1.0
C09 A:M3K1385 4.0 68.5 1.0
CD1 A:LEU215 4.0 81.4 1.0
CB A:VAL211 4.2 79.3 1.0
CB A:LEU215 4.2 83.1 1.0
C A:SER212 4.3 81.0 1.0
CD2 A:LEU115 4.4 76.2 1.0
C A:PHE209 4.4 58.9 1.0
N A:GLY210 4.6 59.5 1.0
O A:GLY210 4.6 75.6 1.0
O1 A:M3K1385 4.7 72.3 1.0
CG1 A:ILE216 4.8 77.6 1.0
N07 A:M3K1385 4.8 70.9 1.0
CG A:LEU215 4.8 83.3 1.0
OG A:SER212 4.9 85.9 1.0
C15 A:M3K1385 5.0 76.8 1.0

Reference:

I.V.Hartung, M.Hitchcock, F.Puehler, R.Neuhaus, A.Scholz, S.Hammer, K.Petersen, G.Siemeister, D.Brittain, R.C.Hillig. Optimization of Allosteric Mek Inhibitors - Part 1: Venturing Into Unexplored Sar Territories Bioorg.Med.Chem.Lett. V. 23 2384 2013.
ISSN: ISSN 0960-894X
PubMed: 23474388
DOI: 10.1016/J.BMCL.2013.02.028
Page generated: Mon Jul 14 20:27:37 2025

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