Fluorine in PDB 3elj: JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor.

All present enzymatic activity of JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor.:
2.7.11.24;

The structure of JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor., PDB code: 3elj was solved by S.Chamberlain, C.Atkins, F.Deanda, M.Dumble, R.Gerding, A.Groy, S.Korenchuk, R.Kumar, H.Lei, R.Mook, G.Moorthy, A.Redman, J.Rowland, L.Shewchuk, G.Vicentini, J.Mosley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.76 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.745, 71.465, 108.692, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 21.5

The binding sites of Fluorine atom in the JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor. (pdb code 3elj). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor., PDB code: 3elj:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:F365 b:14.2 occ:0.50 F A:GS7365 0.0 14.2 0.5 C16 A:GS7365 1.3 14.4 0.5 F A:GS7365 2.2 16.8 0.5 C15 A:GS7365 2.3 14.4 0.5 C17 A:GS7365 2.4 14.4 0.5 C16 A:GS7365 2.4 16.8 0.5 N4 A:GS7365 2.6 13.8 0.5 C17 A:GS7365 2.8 16.7 0.5 C18 A:GS7365 2.8 14.5 0.5 C18 A:GS7365 3.0 16.8 0.5 C A:SER34 3.2 23.0 1.0 C15 A:GS7365 3.2 16.6 0.5 N A:GLY35 3.2 22.9 1.0 O A:SER34 3.2 23.0 1.0 N4 A:GS7365 3.4 17.3 0.5 CA A:GLY35 3.5 22.8 1.0 O4 A:GS7365 3.5 17.5 0.5 C14 A:GS7365 3.6 14.5 0.5 O A:HOH605 3.6 36.7 1.0 C12 A:GS7365 3.6 14.2 0.5 O A:HOH505 3.8 35.5 1.0 C12 A:GS7365 3.8 15.9 0.5 CA A:SER34 3.9 23.1 1.0 O4 A:GS7365 3.9 14.2 0.5 CG2 A:VAL40 4.0 19.2 1.0 N A:SER34 4.1 22.9 1.0 C13 A:GS7365 4.1 14.7 0.5 C14 A:GS7365 4.1 16.7 0.5 C13 A:GS7365 4.3 16.6 0.5 O A:HOH481 4.5 30.5 1.0 C A:GLY33 4.6 22.9 1.0 N3 A:GS7365 4.7 15.0 0.5 O A:GLY38 4.7 22.0 1.0 N3 A:GS7365 4.8 14.2 0.5 CB A:VAL40 4.8 18.6 1.0 C A:GLY35 4.8 22.9 1.0 O A:GLY33 4.9 22.9 1.0

Fluorine binding site 2 out of 2 in the JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of JNK1 Complexed with A Bis-Anilino-Pyrrolopyrimidine Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:F365 b:16.8 occ:0.50 F A:GS7365 0.0 16.8 0.5 C16 A:GS7365 1.3 16.8 0.5 F A:GS7365 2.2 14.2 0.5 C16 A:GS7365 2.3 14.4 0.5 C15 A:GS7365 2.3 16.6 0.5 C17 A:GS7365 2.4 16.7 0.5 N4 A:GS7365 2.5 17.3 0.5 O A:HOH605 2.8 36.7 1.0 C18 A:GS7365 2.8 16.8 0.5 C15 A:GS7365 2.8 14.4 0.5 C17 A:GS7365 2.9 14.4 0.5 N4 A:GS7365 2.9 13.8 0.5 O A:SER155 3.2 16.4 1.0 C18 A:GS7365 3.4 14.5 0.5 C14 A:GS7365 3.6 16.7 0.5 C12 A:GS7365 3.6 15.9 0.5 C14 A:GS7365 3.8 14.5 0.5 C12 A:GS7365 3.8 14.2 0.5 O4 A:GS7365 3.9 17.5 0.5 O A:SER34 4.0 23.0 1.0 O A:HOH612 4.0 41.8 1.0 C13 A:GS7365 4.1 16.6 0.5 C13 A:GS7365 4.2 14.7 0.5 C A:SER155 4.2 15.8 1.0 OD1 A:ASN156 4.4 21.3 1.0 CB A:SER155 4.5 15.3 1.0 C A:SER34 4.5 23.0 1.0 CA A:GLY35 4.6 22.8 1.0 O4 A:GS7365 4.6 14.2 0.5 N A:GLY35 4.8 22.9 1.0 N3 A:GS7365 4.8 15.0 0.5 CA A:SER155 4.8 15.5 1.0 N3 A:GS7365 4.8 14.2 0.5 ND2 A:ASN114 4.9 20.9 1.0 O A:HOH495 5.0 28.3 1.0

S.D.Chamberlain, A.M.Redman, J.W.Wilson, F.Deanda, J.B.Shotwell, R.Gerding, H.Lei, B.Yang, K.L.Stevens, A.M.Hassell, L.M.Shewchuk, M.A.Leesnitzer, J.L.Smith, P.Sabbatini, C.Atkins, A.Groy, J.L.Rowand, R.Kumar, R.A.Mook, G.Moorthy, S.Patnaik. Optimization of 4,6-Bis-Anilino-1H-Pyrrolo[2,3-D]Pyrimidine Igf-1R Tyrosine Kinase Inhibitors Towards Jnk Selectivity. Bioorg.Med.Chem.Lett. V. 19 360 2009.
ISSN: ISSN 0960-894X
PubMed: 19071018
DOI: 10.1016/J.BMCL.2008.11.077