Fluorine in PDB 7jus: Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

Enzymatic activity of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

All present enzymatic activity of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib:
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 Cobimetinib, PDB code: 7jus 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)*	46.72 / 2.99
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	140.000, 140.000, 220.000, 90.00, 90.00, 120.00
*R / R_free (%)*	24.8 / 26.5

Other elements in 7jus:

The structure of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib 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 Cobimetinib (pdb code 7jus). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib, PDB code: 7jus:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 7jus

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Fluorine Binding Sites List in 7jus

Fluorine binding site 1 out of 3 in the Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

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 Cobimetinib within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:F501 b:0.9 occ:1.00	F07	C:VKD501	0.0	0.9	1.0
	C06	C:VKD501	1.4	0.1	1.0
	C05	C:VKD501	2.4	0.9	1.0
	C08	C:VKD501	2.4	0.0	1.0
	F09	C:VKD501	2.7	0.7	1.0
	CG2	C:VAL211	3.3	0.9	1.0
	N	C:SER212	3.5	0.4	1.0
	N	C:VAL211	3.5	0.5	1.0
	C04	C:VKD501	3.6	0.6	1.0
	CD1	C:LEU215	3.7	0.3	1.0
	C10	C:VKD501	3.7	0.7	1.0
	CB	C:SER212	3.8	0.7	1.0
	O	C:PHE209	3.9	0.8	1.0
	CA	C:SER212	4.2	0.2	1.0
	O	C:SER212	4.2	1.0	1.0
	CA	C:VAL211	4.2	0.9	1.0
	C03	C:VKD501	4.2	0.1	1.0
	CB	C:VAL211	4.2	0.8	1.0
	C	C:VAL211	4.3	0.4	1.0
	CD2	C:LEU115	4.3	1.0	1.0
	C	C:GLY210	4.4	0.3	1.0
	CB	C:LEU215	4.4	0.0	1.0
	CG	C:LEU215	4.5	0.6	1.0
	CG1	C:VAL211	4.5	0.9	1.0
	CA	C:GLY210	4.5	0.7	1.0
	C	C:SER212	4.6	0.7	1.0
	CD2	C:LEU215	4.8	0.6	1.0
	OG	C:SER212	4.8	0.5	1.0
	N11	C:VKD501	4.9	0.1	1.0
	C	C:PHE209	4.9	0.1	1.0
	C13	C:VKD501	5.0	0.4	1.0

Fluorine binding site 2 out of 3 in 7jus

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Fluorine Binding Sites List in 7jus

Fluorine binding site 2 out of 3 in the Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

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 KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:F501 b:0.7 occ:1.00	F09	C:VKD501	0.0	0.7	1.0
	C08	C:VKD501	1.4	0.0	1.0
	C06	C:VKD501	2.4	0.1	1.0
	C10	C:VKD501	2.4	0.7	1.0
	C13	C:VKD501	2.7	0.4	1.0
	F07	C:VKD501	2.7	0.9	1.0
	N11	C:VKD501	2.9	0.1	1.0
	C12	C:VKD501	3.0	0.2	1.0
	CD1	C:ILE141	3.4	0.0	1.0
	CD2	C:LEU115	3.6	1.0	1.0
	C05	C:VKD501	3.6	0.9	1.0
	C03	C:VKD501	3.7	0.1	1.0
	C14	C:VKD501	3.7	0.3	1.0
	CG2	C:VAL211	3.8	0.9	1.0
	O	C:PHE209	4.0	0.8	1.0
	C04	C:VKD501	4.1	0.6	1.0
	C18	C:VKD501	4.2	1.0	1.0
	CD1	C:LEU118	4.4	0.0	1.0
	CD1	C:LEU215	4.4	0.3	1.0
	CG1	C:VAL211	4.5	0.9	1.0
	C15	C:VKD501	4.7	0.8	1.0
	CB	C:VAL211	4.8	0.8	1.0
	CG1	C:ILE141	4.8	0.4	1.0
	C17	C:VKD501	4.9	0.4	1.0
	C02	C:VKD501	5.0	0.4	1.0
	N	C:VAL211	5.0	0.5	1.0

Fluorine binding site 3 out of 3 in 7jus

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Fluorine Binding Sites List in 7jus

Fluorine binding site 3 out of 3 in the Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of KSR2:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Cobimetinib within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:F501 b:0.8 occ:1.00	F19	C:VKD501	0.0	0.8	1.0
	C18	C:VKD501	1.4	1.0	1.0
	C12	C:VKD501	2.4	0.2	1.0
	C17	C:VKD501	2.4	0.4	1.0
	OD2	C:ASP208	2.8	0.1	1.0
	N11	C:VKD501	2.8	0.1	1.0
	C13	C:VKD501	3.6	0.4	1.0
	C15	C:VKD501	3.7	0.8	1.0
	CG	C:ASP208	4.0	0.8	1.0
	SD	C:MET143	4.0	0.5	1.0
	CG2	C:ILE141	4.1	0.4	1.0
	O01	C:VKD501	4.1	0.9	1.0
	CD	C:LYS97	4.1	0.9	1.0
	C14	C:VKD501	4.2	0.3	1.0
	C10	C:VKD501	4.3	0.7	1.0
	CE	C:LYS97	4.4	0.6	1.0
	CE	C:MET143	4.5	0.4	1.0
	CB	C:ILE141	4.5	0.6	1.0
	CA	C:ASP208	4.5	0.4	1.0
	CD1	C:ILE141	4.5	0.0	1.0
	SG	C:CYS207	4.6	0.3	1.0
	N	C:ASP208	4.6	0.4	1.0
	CB	C:LYS97	4.7	0.2	1.0
	OD1	C:ASP208	4.7	0.6	1.0
	CG	C:LYS97	4.7	0.5	1.0
	CB	C:ASP208	4.8	0.4	1.0
	C02	C:VKD501	4.9	0.4	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: Tue Jul 15 20:35:29 2025

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