Fluorine in PDB 3fqs: Crystal Structure of Spleen Tyrosine Kinase Complexed with R406

All present enzymatic activity of Crystal Structure of Spleen Tyrosine Kinase Complexed with R406:
2.7.10.2;

The structure of Crystal Structure of Spleen Tyrosine Kinase Complexed with R406, PDB code: 3fqs was solved by A.Kuglstatter, A.G.Villasenor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.52 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.971, 85.079, 91.144, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 25.3

The binding sites of Fluorine atom in the Crystal Structure of Spleen Tyrosine Kinase Complexed with R406 (pdb code 3fqs). 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 Spleen Tyrosine Kinase Complexed with R406, PDB code: 3fqs:

Fluorine binding site 1 out of 1 in the Crystal Structure of Spleen Tyrosine Kinase Complexed with R406


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 Spleen Tyrosine Kinase Complexed with R406 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:36.1 occ:1.00 F25 A:5851 0.0 36.1 1.0 C11 A:5851 1.3 37.8 1.0 C4 A:5851 2.4 38.8 1.0 C22 A:5851 2.4 36.7 1.0 N10 A:5851 2.7 42.8 1.0 N2 A:5851 3.6 38.0 1.0 N17 A:5851 3.6 37.5 1.0 O A:HOH1077 3.8 51.8 1.0 CE A:MET448 3.8 45.9 1.0 SD A:MET448 3.8 44.4 1.0 CB A:ALA400 3.9 36.7 1.0 O A:HOH2050 3.9 44.7 1.0 CB A:MET448 4.0 40.4 1.0 C7 A:5851 4.0 37.0 1.0 CG1 A:VAL433 4.1 37.0 1.0 C14 A:5851 4.1 45.7 1.0 CD1 A:LEU501 4.2 27.1 1.0 O A:GLU449 4.2 39.2 1.0 CG A:MET448 4.6 41.0 1.0 N6 A:5851 4.7 47.0 1.0

A.G.Villasenor, R.Kondru, H.Ho, S.Wang, E.Papp, D.Shaw, J.W.Barnett, M.F.Browner, A.Kuglstatter. Structural Insights For Design of Potent Spleen Tyrosine Kinase Inhibitors From Crystallographic Analysis of Three Inhibitor Complexes. Chem.Biol.Drug Des. V. 73 466 2009.
ISSN: ISSN 1747-0277
PubMed: 19220318
DOI: 10.1111/J.1747-0285.2009.00785.X