Fluorine in PDB 7jv1: Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1

Enzymatic activity of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1

All present enzymatic activity of Crystal Structure of KSR1: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 KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1, PDB code: 7jv1 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)*	46.20 / 3.62
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	137.000, 137.000, 221.000, 90.00, 90.00, 120.00
*R / R_free (%)*	27.7 / 30.3

Other elements in 7jv1:

The structure of Crystal Structure of KSR1:MEK1 in Complex with Amp-Pnp, and Allosteric Mek Inhibitor Aps-9-95-1 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 Aps-9-95-1 (pdb code 7jv1). 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 Aps-9-95-1, PDB code: 7jv1:

Fluorine binding site 1 out of 1 in 7jv1

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Fluorine Binding Sites List in 7jv1

Fluorine binding site 1 out of 1 in the Crystal Structure of KSR1: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 KSR1: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:0.4 occ:1.00	F31	C:VKG402	0.0	0.4	1.0
	C30	C:VKG402	1.4	0.1	1.0
	O20	C:VKG402	2.3	0.7	1.0
	C29	C:VKG402	2.4	0.4	1.0
	C24	C:VKG402	2.4	0.0	1.0
	OD1	C:ASP208	2.6	0.1	1.0
	N23	C:VKG402	2.9	0.6	1.0
	C19	C:VKG402	3.4	0.4	1.0
	CG	C:ASP208	3.5	0.7	1.0
	C25	C:VKG402	3.7	0.1	1.0
	C27	C:VKG402	3.7	0.6	1.0
	CA	C:ASP208	3.7	0.4	1.0
	C22	C:VKG402	4.0	0.6	1.0
	CB	C:ASP208	4.1	0.4	1.0
	C26	C:VKG402	4.2	0.5	1.0
	C21	C:VKG402	4.2	0.4	1.0
	CD1	C:ILE141	4.2	0.2	1.0
	N	C:ASP208	4.2	0.5	1.0
	N15	C:VKG402	4.3	0.2	1.0
	C16	C:VKG402	4.3	0.3	1.0
	OD2	C:ASP208	4.5	0.1	1.0
	C17	C:VKG402	4.6	0.4	1.0
	C	C:ASP208	4.8	0.8	1.0
	CD	C:LYS97	4.8	0.9	1.0
	CE	C:LYS97	4.9	0.3	1.0
	NZ	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: Fri Aug 2 08:03:49 2024

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