Fluorine in PDB 7jux: Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib

Enzymatic activity of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib

All present enzymatic activity of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib:
2.7.11.1; 2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib, PDB code: 7jux was solved by Z.M.Khan, A.C.Dar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.00 / 3.34
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 137.470, 137.470, 221.800, 90.00, 90.00, 120.00
R / Rfree (%) 26.4 / 28.3

Other elements in 7jux:

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib 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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib (pdb code 7jux). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib, PDB code: 7jux:

Fluorine binding site 1 out of 1 in 7jux

Go back to Fluorine Binding Sites List in 7jux
Fluorine binding site 1 out of 1 in the Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib


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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Trametinib within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F402

b:0.8
occ:1.00
 F18 C:QOM402 0.0 0.8 1.0
C12 C:QOM402 1.4 0.8 1.0
C13 C:QOM402 2.4 0.3 1.0
C11 C:QOM402 2.4 0.1 1.0
O20 C:QOM402 2.6 0.4 1.0
N10 C:QOM402 2.9 0.1 1.0
OD1 C:ASP208 2.9 0.5 1.0
C16 C:QOM402 3.7 0.1 1.0
C14 C:QOM402 3.7 0.4 1.0
C19 C:QOM402 3.7 0.7 1.0
CG C:ASP208 4.0 1.0 1.0
CD1 C:ILE141 4.1 0.3 1.0
CA C:ASP208 4.1 0.1 1.0
C05 C:QOM402 4.1 0.1 1.0
C15 C:QOM402 4.2 0.6 1.0
N C:ASP208 4.4 0.2 1.0
C36 C:QOM402 4.4 0.9 1.0
C04 C:QOM402 4.5 0.4 1.0
CG2 C:ILE141 4.5 0.1 1.0
CE C:MET143 4.6 0.1 1.0
CB C:ASP208 4.7 0.2 1.0
N21 C:QOM402 4.7 1.0 1.0
C35 C:QOM402 4.7 0.2 1.0
CB C:ILE141 4.8 0.6 1.0
CD C:LYS97 4.9 0.3 1.0
SD C:MET143 4.9 0.0 1.0
OD2 C:ASP208 5.0 0.0 1.0

Reference:

Z.M.Khan, A.M.Real, W.M.Marsiglia, A.Chow, M.E.Duffy, J.R.Yerabolu, A.P.Scopton, A.C.Dar. Structural Basis For the Action of the Drug Trametinib at Ksr-Bound Mek. Nature 2020.
ISSN: ESSN 1476-4687
PubMed: 32927473
DOI: 10.1038/S41586-020-2760-4
Page generated: Sun Dec 13 13:58:43 2020

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