Fluorine in PDB 2gtn: Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717

All present enzymatic activity of Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717:
2.7.11.24;

The structure of Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717, PDB code: 2gtn was solved by R.L.Walter, M.J.Mekel, A.G.Evdokimov, M.E.Pokross, M.Sabat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.986, 74.554, 78.029, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.8

The binding sites of Fluorine atom in the Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717 (pdb code 2gtn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717, PDB code: 2gtn:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717 within 5.0Å range: probe atom residue distance (Å) B Occ A:F354 b:26.9 occ:1.00 F40 A:LIE354 0.0 26.9 1.0 C36 A:LIE354 1.3 24.4 1.0 C39 A:LIE354 2.4 25.2 1.0 C34 A:LIE354 2.4 25.4 1.0 N12 A:LIE354 2.8 23.9 1.0 C10 A:LIE354 3.2 22.9 1.0 CB A:ALA51 3.2 23.0 1.0 N11 A:LIE354 3.2 21.1 1.0 O A:ALA51 3.5 24.2 1.0 C A:ALA51 3.5 23.2 1.0 CB A:LYS53 3.6 24.4 1.0 C35 A:LIE354 3.6 26.0 1.0 C37 A:LIE354 3.7 28.2 1.0 N A:LYS53 3.7 22.5 1.0 CG1 A:VAL38 3.7 27.9 1.0 OG1 A:THR106 3.8 27.8 1.0 N A:VAL52 3.9 22.6 1.0 C A:VAL52 4.0 23.8 1.0 CA A:ALA51 4.0 24.2 1.0 C38 A:LIE354 4.1 29.0 1.0 CA A:LYS53 4.1 23.4 1.0 CG2 A:VAL38 4.1 27.5 1.0 N8 A:LIE354 4.2 23.9 1.0 C3 A:LIE354 4.3 23.2 1.0 O A:LEU104 4.3 21.5 1.0 CA A:VAL52 4.3 23.5 1.0 O A:VAL52 4.4 22.4 1.0 CB A:VAL38 4.6 27.4 1.0 CG A:LYS53 4.6 27.6 1.0 C6 A:LIE354 4.7 23.4 1.0 CG2 A:THR106 4.8 31.1 1.0 N A:THR106 4.9 24.1 1.0 CD A:LYS53 4.9 32.1 1.0 CB A:THR106 4.9 25.4 1.0

Fluorine binding site 2 out of 3 in the Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717 within 5.0Å range: probe atom residue distance (Å) B Occ A:F354 b:35.8 occ:1.00 F19 A:LIE354 0.0 35.8 1.0 C15 A:LIE354 1.3 31.7 1.0 C13 A:LIE354 2.3 30.6 1.0 C18 A:LIE354 2.4 31.8 1.0 O9 A:LIE354 2.6 30.4 1.0 C A:GLY110 3.1 31.9 1.0 CA A:GLY110 3.1 31.7 1.0 O A:GLY110 3.2 31.6 1.0 N A:GLY110 3.3 29.7 1.0 C5 A:LIE354 3.5 25.1 1.0 CD1 A:LEU108 3.5 29.4 1.0 C16 A:LIE354 3.6 33.0 1.0 C14 A:LIE354 3.6 34.7 1.0 N A:ALA111 3.7 29.3 1.0 N2 A:LIE354 4.0 24.4 1.0 C17 A:LIE354 4.1 32.5 1.0 CG A:LEU108 4.1 28.5 1.0 N4 A:LIE354 4.3 24.5 1.0 CG1 A:VAL30 4.4 38.3 1.0 CA A:ALA111 4.4 29.7 1.0 F20 A:LIE354 4.6 30.8 1.0 C A:MET109 4.6 28.4 1.0 CD2 A:LEU108 4.7 30.5 1.0 CG2 A:VAL30 4.7 38.9 1.0 N A:MET109 4.9 25.9 1.0

Fluorine binding site 3 out of 3 in the Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Mutated Map Kinase P38 (Mus Musculus) in Complex with Inhbitor Pg- 951717 within 5.0Å range: probe atom residue distance (Å) B Occ A:F354 b:30.8 occ:1.00 F20 A:LIE354 0.0 30.8 1.0 C16 A:LIE354 1.3 33.0 1.0 C13 A:LIE354 2.3 30.6 1.0 C17 A:LIE354 2.4 32.5 1.0 O9 A:LIE354 2.7 30.4 1.0 N2 A:LIE354 2.9 24.4 1.0 C5 A:LIE354 3.1 25.1 1.0 O A:ALA111 3.2 27.1 1.0 CB A:ALA157 3.5 22.9 1.0 C15 A:LIE354 3.6 31.7 1.0 C A:ALA111 3.6 29.5 1.0 C14 A:LIE354 3.6 34.7 1.0 CB A:ASP112 3.9 32.1 1.0 CA A:ALA157 3.9 23.1 1.0 O A:HOH368 3.9 27.5 1.0 N A:ASP112 3.9 30.1 1.0 C6 A:LIE354 4.0 23.4 1.0 CD1 A:LEU167 4.0 27.8 1.0 N4 A:LIE354 4.1 24.5 1.0 CA A:ASP112 4.1 31.6 1.0 C18 A:LIE354 4.1 31.8 1.0 C25 A:LIE354 4.2 27.1 1.0 CA A:ALA111 4.4 29.7 1.0 N A:ALA111 4.5 29.3 1.0 F19 A:LIE354 4.6 35.8 1.0 OD2 A:ASP112 4.6 36.6 1.0 N8 A:LIE354 4.7 23.9 1.0 CG A:ASP112 4.7 32.4 1.0 N A:ALA157 4.7 21.3 1.0 C7 A:LIE354 4.7 26.1 1.0 C26 A:LIE354 4.8 28.6 1.0 C3 A:LIE354 4.9 23.2 1.0 C1 A:LIE354 4.9 26.4 1.0 O A:LEU156 4.9 23.0 1.0

M.Sabat, J.C.Vanrens, M.P.Clark, T.A.Brugel, J.Maier, R.G.Bookland, M.J.Laufersweiler, S.K.Laughlin, A.Golebiowski, B.De, L.C.Hsieh, R.L.Walter, M.J.Mekel, M.J.Janusz. The Development of Novel C-2, C-8, and N-9 Trisubstituted Purines As Inhibitors of Tnf-Alpha Production. Bioorg.Med.Chem.Lett. V. 16 4360 2006.
ISSN: ISSN 0960-894X
PubMed: 16750367
DOI: 10.1016/J.BMCL.2006.05.050