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Fluorine in PDB 3pp1: Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp

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

All present enzymatic activity of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp:
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 Mgatp, PDB code: 3pp1 was solved by D.R.Dougan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.70
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 82.086, 82.086, 129.254, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 21.9

Other elements in 3pp1:

The structure of Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp 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 Mgatp (pdb code 3pp1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp, PDB code: 3pp1:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 3pp1

Go back to Fluorine Binding Sites List in 3pp1
Fluorine binding site 1 out of 2 in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp


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 Mgatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F500

b:35.7
occ:1.00
F25 A:IZG500 0.0 35.7 1.0
C24 A:IZG500 1.4 41.8 1.0
C18 A:IZG500 2.4 41.2 1.0
C23 A:IZG500 2.4 43.9 1.0
N17 A:IZG500 2.7 44.4 1.0
OD1 A:ASP208 3.3 43.7 1.0
CD A:LYS97 3.5 44.0 1.0
CG2 A:ILE141 3.5 38.4 1.0
C19 A:IZG500 3.7 42.4 1.0
C21 A:IZG500 3.7 46.5 1.0
O14 A:IZG500 3.7 55.6 1.0
CD1 A:ILE141 3.9 42.3 1.0
SD A:MET143 3.9 51.7 1.0
CB A:ILE141 4.0 41.5 1.0
C16 A:IZG500 4.1 47.9 1.0
C20 A:IZG500 4.1 45.6 1.0
CE A:LYS97 4.2 45.7 1.0
CB A:LYS97 4.4 40.0 1.0
CG A:MET143 4.5 47.9 1.0
NZ A:LYS97 4.5 45.5 1.0
CG A:LYS97 4.5 41.7 1.0
CE A:MET143 4.5 51.2 1.0
CG A:ASP208 4.5 40.3 1.0
CG1 A:ILE141 4.6 42.0 1.0
C13 A:IZG500 4.7 56.8 1.0
N A:ASP208 4.9 40.8 1.0
CA A:ASP208 4.9 38.6 1.0
C15 A:IZG500 4.9 52.0 1.0
F27 A:IZG500 5.0 50.3 1.0

Fluorine binding site 2 out of 2 in 3pp1

Go back to Fluorine Binding Sites List in 3pp1
Fluorine binding site 2 out of 2 in the Crystal Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp


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 the Human Mitogen-Activated Protein Kinase Kinase 1 (Mek 1) in Complex with Ligand and Mgatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F500

b:50.3
occ:1.00
F27 A:IZG500 0.0 50.3 1.0
C26 A:IZG500 1.3 48.6 1.0
C28 A:IZG500 2.4 49.3 1.0
C16 A:IZG500 2.4 47.9 1.0
O29 A:IZG500 2.6 48.1 1.0
C19 A:IZG500 2.7 42.4 1.0
N17 A:IZG500 2.8 44.4 1.0
C18 A:IZG500 3.0 41.2 1.0
CG2 A:VAL211 3.5 53.7 1.0
CD2 A:LEU115 3.6 50.9 1.0
O A:PHE209 3.6 39.1 1.0
N2 A:IZG500 3.6 50.6 1.0
C15 A:IZG500 3.7 52.0 1.0
C20 A:IZG500 3.8 45.6 1.0
C3 A:IZG500 4.1 53.5 1.0
C24 A:IZG500 4.2 41.8 1.0
CD1 A:ILE141 4.2 42.3 1.0
N A:VAL211 4.3 47.7 1.0
CD1 A:LEU118 4.3 44.0 1.0
CD2 A:LEU215 4.6 47.6 1.0
CB A:VAL211 4.7 53.5 1.0
C1 A:IZG500 4.8 49.4 1.0
C A:PHE209 4.8 38.1 1.0
C21 A:IZG500 4.8 46.5 1.0
C13 A:IZG500 4.9 56.8 1.0
CD2 A:LEU118 4.9 45.1 1.0
C23 A:IZG500 5.0 43.9 1.0
F25 A:IZG500 5.0 35.7 1.0

Reference:

Q.Dong, D.R.Dougan, X.Gong, P.Halkowycz, B.Jin, T.Kanouni, S.M.O'connell, N.Scorah, L.Shi, M.B.Wallace, F.Zhou. Discovery of Tak-733, A Potent and Selective Mek Allosteric Site Inhibitor For the Treatment of Cancer. Bioorg.Med.Chem.Lett. V. 21 1315 2011.
ISSN: ISSN 0960-894X
PubMed: 21310613
DOI: 10.1016/J.BMCL.2011.01.071
Page generated: Wed Jul 31 21:48:41 2024

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