Fluorine in PDB 7juv: Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1

Enzymatic activity of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1

All present enzymatic activity of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1:
2.7.11.1; 2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1, PDB code: 7juv was solved by Z.M.Khan, A.C.Dar, A.P.Scopton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.77 / 3.36
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 139.000, 139.000, 222.000, 90.00, 90.00, 120.00
R / Rfree (%) 24.2 / 25.5

Other elements in 7juv:

The structure of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Iodine (I) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1 (pdb code 7juv). 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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1, PDB code: 7juv:

Fluorine binding site 1 out of 1 in 7juv

Go back to Fluorine Binding Sites List in 7juv
Fluorine binding site 1 out of 1 in the Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1


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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F402

b:0.9
occ:1.00
 F31 C:VKG402 0.0 0.9 1.0
C30 C:VKG402 1.4 0.7 1.0
C29 C:VKG402 2.4 0.0 1.0
C24 C:VKG402 2.4 0.5 1.0
O20 C:VKG402 2.6 0.5 1.0
OD1 C:ASP208 2.6 0.6 1.0
N23 C:VKG402 2.9 0.9 1.0
NZ C:LYS97 3.4 0.6 1.0
CD C:LYS97 3.5 1.0 1.0
C25 C:VKG402 3.7 0.2 1.0
C27 C:VKG402 3.7 0.6 1.0
C19 C:VKG402 3.7 0.1 1.0
CG C:ASP208 3.7 0.1 1.0
CE C:LYS97 3.9 0.5 1.0
CD1 C:ILE141 3.9 0.4 1.0
CE C:MET143 4.1 0.8 1.0
C22 C:VKG402 4.1 0.0 1.0
C26 C:VKG402 4.1 0.3 1.0
CA C:ASP208 4.3 0.8 1.0
C21 C:VKG402 4.4 0.4 1.0
CG2 C:ILE141 4.5 0.9 1.0
CB C:ASP208 4.5 0.6 1.0
OD2 C:ASP208 4.6 0.4 1.0
N15 C:VKG402 4.6 0.5 1.0
CB C:ILE141 4.6 0.4 1.0
C16 C:VKG402 4.6 0.9 1.0
N C:ASP208 4.8 0.4 1.0
CG1 C:ILE141 4.9 0.2 1.0
CG C:LYS97 4.9 0.8 1.0
CB C:LYS97 5.0 0.2 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 13:58:31 2020

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