Fluorine in PDB 2gtm: Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579

All present enzymatic activity of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579:
2.7.11.24;

The structure of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579, PDB code: 2gtm 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)	40.80 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.876, 73.627, 76.160, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 26.1

The structure of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 (pdb code 2gtm). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579, PDB code: 2gtm:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 within 5.0Å range: probe atom residue distance (Å) B Occ A:F353 b:38.8 occ:1.00 F28 A:LID353 0.0 38.8 1.0 C16 A:LID353 1.4 39.0 1.0 C17 A:LID353 2.4 41.5 1.0 C15 A:LID353 2.5 40.3 1.0 N14 A:LID353 2.9 40.1 1.0 N4 A:LID353 2.9 34.0 1.0 C5 A:LID353 3.2 34.5 1.0 O A:ALA111 3.5 37.7 1.0 C18 A:LID353 3.7 42.4 1.0 C20 A:LID353 3.8 45.0 1.0 C A:ALA111 3.8 39.5 1.0 CB A:ALA157 4.0 28.0 1.0 C3 A:LID353 4.0 28.0 1.0 N A:ASP112 4.1 40.2 1.0 CB A:ASP112 4.1 41.6 1.0 CD1 A:LEU167 4.1 33.7 1.0 O A:HOH452 4.2 37.8 1.0 N6 A:LID353 4.3 40.0 1.0 CA A:ASP112 4.3 42.0 1.0 C19 A:LID353 4.3 42.8 1.0 CA A:ALA157 4.3 28.5 1.0 C10 A:LID353 4.6 34.5 1.0 CA A:ALA111 4.6 39.2 1.0 N7 A:LID353 4.6 33.6 1.0 N A:ALA111 4.6 39.4 1.0 C2 A:LID353 4.8 28.3 1.0 C11 A:LID353 4.8 37.7 1.0 F27 A:LID353 4.9 48.7 1.0 C1 A:LID353 5.0 33.3 1.0

Fluorine binding site 2 out of 2 in the Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mutated Mouse P38 Map Kinase Domain in Complex with Inhibitor Pg- 892579 within 5.0Å range: probe atom residue distance (Å) B Occ A:F353 b:48.7 occ:1.00 F27 A:LID353 0.0 48.7 1.0 C20 A:LID353 1.3 45.0 1.0 C15 A:LID353 2.3 40.3 1.0 C19 A:LID353 2.4 42.8 1.0 N14 A:LID353 2.6 40.1 1.0 CA A:GLY110 3.2 40.9 1.0 N A:GLY110 3.5 38.0 1.0 C5 A:LID353 3.6 34.5 1.0 C18 A:LID353 3.6 42.4 1.0 C A:GLY110 3.6 40.2 1.0 O A:HOH497 3.7 56.7 1.0 C16 A:LID353 3.7 39.0 1.0 CD1 A:LEU108 3.7 35.3 1.0 O A:GLY110 3.9 39.4 1.0 CG1 A:VAL30 3.9 41.8 1.0 C17 A:LID353 4.2 41.5 1.0 N4 A:LID353 4.3 34.0 1.0 N A:ALA111 4.3 39.4 1.0 CG2 A:VAL30 4.3 42.3 1.0 CG A:LEU108 4.5 34.0 1.0 N6 A:LID353 4.6 40.0 1.0 C A:MET109 4.8 36.9 1.0 CB A:VAL30 4.8 40.0 1.0 F28 A:LID353 4.9 38.8 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