Fluorine in PDB 1o46: Crystal Structure of SH2 in Complex with RU90395.

All present enzymatic activity of Crystal Structure of SH2 in Complex with RU90395.:
2.7.1.112;

The structure of Crystal Structure of SH2 in Complex with RU90395., PDB code: 1o46 was solved by G.Lange, P.Loenze, A.Liesum, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	26.587, 58.554, 64.188, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / n/a

The binding sites of Fluorine atom in the Crystal Structure of SH2 in Complex with RU90395. (pdb code 1o46). 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 SH2 in Complex with RU90395., PDB code: 1o46:

Fluorine binding site 1 out of 1 in the Crystal Structure of SH2 in Complex with RU90395.


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 SH2 in Complex with RU90395. within 5.0Å range: probe atom residue distance (Å) B Occ A:F300 b:27.2 occ:1.00 F80 A:903300 0.0 27.2 1.0 C40 A:903300 1.6 30.0 1.0 C41 A:903300 2.2 30.0 1.0 O43 A:903300 2.2 30.9 1.0 C4 A:903300 2.8 32.6 1.0 OG A:SER36 2.8 21.1 1.0 C75 A:903300 2.9 25.6 1.0 O76 A:903300 3.0 26.1 1.0 NZ A:LYS62 3.2 33.8 1.0 O42 A:903300 3.5 30.3 1.0 C3 A:903300 3.6 34.9 1.0 CB A:SER36 3.6 18.7 1.0 OG1 A:THR38 3.7 29.8 1.0 C5 A:903300 3.7 36.6 1.0 N A:GLU37 3.7 22.2 1.0 N A:THR38 3.8 29.9 1.0 O39 A:903300 3.8 34.8 1.0 CE A:LYS62 3.8 34.1 1.0 CA A:SER36 4.0 18.5 1.0 O77 A:903300 4.1 21.8 1.0 C A:SER36 4.1 19.2 1.0 SG A:CYS44 4.1 32.6 1.0 C37 A:903300 4.2 37.5 1.0 N A:THR39 4.4 36.8 1.0 CA A:THR38 4.5 31.9 1.0 CA A:GLU37 4.6 24.5 1.0 C A:GLU37 4.7 28.1 1.0 CB A:THR38 4.7 32.0 1.0 CB A:GLU37 4.7 22.3 1.0 OG1 A:THR39 4.7 39.2 1.0 C2 A:903300 4.8 35.0 1.0 CD A:LYS62 4.9 32.4 1.0 C6 A:903300 4.9 37.2 1.0 C A:THR38 5.0 35.5 1.0

G.Lange, D.Lesuisse, P.Deprez, B.Schoot, P.Loenze, D.Benard, J.P.Marquette, P.Broto, E.Sarubbi, E.Mandine. Requirements For Specific Binding of Low Affinity Inhibitor Fragments to the SH2 Domain of (PP60)Src Are Identical to Those For High Affinity Binding of Full Length Inhibitors. J.Med.Chem. V. 46 5184 2003.
ISSN: ISSN 0022-2623
PubMed: 14613321
DOI: 10.1021/JM020970S