Fluorine in PDB 3mbl: Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp

Enzymatic activity of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp

All present enzymatic activity of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp:
2.7.12.2;

Protein crystallography data

The structure of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp, PDB code: 3mbl was solved by D.R.Dougan, C.D.Mol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 2.60
*Space group*	P 6₂
*Cell size a, b, c (Å), α, β, γ (°)*	81.982, 81.982, 129.928, 90.00, 90.00, 120.00
*R / R_free (%)*	16.6 / 21.5

Other elements in 3mbl:

The structure of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp 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 Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp (pdb code 3mbl). 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 the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp, PDB code: 3mbl:

Fluorine binding site 1 out of 1 in 3mbl

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Fluorine Binding Sites List in 3mbl

Fluorine binding site 1 out of 1 in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp

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 Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgadp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F7 b:66.4 occ:1.00	F7	A:LSG7	0.0	66.4	1.0
	C6	A:LSG7	1.3	66.8	1.0
	C1	A:LSG7	2.4	61.3	1.0
	C5	A:LSG7	2.4	66.1	1.0
	N9	A:LSG7	2.7	60.8	1.0
	OD1	A:ASP208	3.0	60.8	1.0
	CD	A:LYS97	3.4	57.2	1.0
	CE	A:LYS97	3.6	62.5	1.0
	C4	A:LSG7	3.7	68.3	1.0
	C2	A:LSG7	3.7	76.5	1.0
	SD	A:MET143	3.7	67.8	1.0
	O16	A:LSG7	3.7	55.8	1.0
	CG2	A:ILE141	3.7	57.0	1.0
	CD1	A:ILE141	4.0	65.6	1.0
	CB	A:ILE141	4.0	59.8	1.0
	C10	A:LSG7	4.0	62.5	1.0
	C3	A:LSG7	4.1	60.1	1.0
	CG	A:ASP208	4.3	60.4	1.0
	CB	A:LYS97	4.3	57.6	1.0
	SG	A:CYS207	4.3	59.9	0.3
	CG	A:MET143	4.4	61.4	1.0
	CG	A:LYS97	4.4	57.9	1.0
	NZ	A:LYS97	4.4	63.1	1.0
	O	A:HOH650	4.6	64.9	1.0
	CG1	A:ILE141	4.6	63.8	1.0
	C15	A:LSG7	4.7	62.3	1.0
	N	A:ASP208	4.8	53.7	1.0
	CA	A:ASP208	4.8	56.9	1.0
	CE	A:MET143	4.9	69.9	1.0
	C14	A:LSG7	4.9	56.6	1.0

Reference:

M.B.Wallace, M.E.Adams, T.Kanouni, C.D.Mol, D.R.Dougan, V.A.Feher, S.M.O'connell, L.Shi, P.Halkowycz, Q.Dong. Structure-Based Design and Synthesis of Pyrrole Derivatives As Mek Inhibitors. Bioorg.Med.Chem.Lett. V. 20 4156 2010.
ISSN: ISSN 0960-894X
PubMed: 20621728
DOI: 10.1016/J.BMCL.2010.05.058

Page generated: Wed Jul 31 20:41:07 2024

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