Fluorine in PDB 4xg3: Crystal Structure of An Inhibitor-Bound Syk

All present enzymatic activity of Crystal Structure of An Inhibitor-Bound Syk:
2.7.10.2;

The structure of Crystal Structure of An Inhibitor-Bound Syk, PDB code: 4xg3 was solved by S.J.Lee, J.Choi, B.G.Han, H.Song, J.S.Koh, B.I.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.05 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	40.163, 42.326, 87.457, 99.73, 90.83, 100.30
R / Rfree (%)	19.8 / 22.6

The binding sites of Fluorine atom in the Crystal Structure of An Inhibitor-Bound Syk (pdb code 4xg3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of An Inhibitor-Bound Syk, PDB code: 4xg3:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of An Inhibitor-Bound Syk


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 An Inhibitor-Bound Syk within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:34.9 occ:1.00 F5 A:X3G701 0.0 34.9 1.0 C5 A:X3G701 1.3 36.2 1.0 C6 A:X3G701 2.3 36.1 1.0 C4 A:X3G701 2.4 38.0 1.0 CAL A:X3G701 2.8 40.9 1.0 NBG A:X3G701 2.9 40.4 1.0 CG1 A:VAL433 3.5 39.3 1.0 N1 A:X3G701 3.6 37.1 1.0 N3 A:X3G701 3.6 37.7 1.0 CB A:MET448 3.7 39.0 1.0 SD A:MET448 3.8 42.3 1.0 CE A:MET448 3.9 42.0 1.0 CB A:ALA400 3.9 34.4 1.0 O A:HOH832 4.0 40.2 1.0 O A:GLU449 4.1 32.6 1.0 CAX A:X3G701 4.1 40.8 1.0 C2 A:X3G701 4.1 38.1 1.0 CD1 A:LEU501 4.1 30.5 1.0 CAM A:X3G701 4.2 41.1 1.0 CG A:MET448 4.3 40.2 1.0 CG2 A:VAL433 4.4 38.8 1.0 CB A:VAL433 4.5 37.5 1.0 O A:ALA400 4.8 36.0 1.0 CBA A:X3G701 4.8 41.3 1.0 CA A:MET448 4.9 37.2 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of An Inhibitor-Bound Syk


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of An Inhibitor-Bound Syk within 5.0Å range: probe atom residue distance (Å) B Occ B:F701 b:31.9 occ:1.00 F5 B:X3G701 0.0 31.9 1.0 C5 B:X3G701 1.4 33.6 1.0 C6 B:X3G701 2.4 33.2 1.0 C4 B:X3G701 2.4 33.8 1.0 CAL B:X3G701 2.8 31.6 1.0 NBG B:X3G701 2.9 32.9 1.0 CG1 B:VAL433 3.4 32.7 1.0 N1 B:X3G701 3.6 34.5 1.0 SD B:MET448 3.6 28.4 1.0 N3 B:X3G701 3.6 34.9 1.0 CB B:MET448 3.6 29.5 1.0 CE B:MET448 3.8 30.2 1.0 CB B:ALA400 3.9 33.3 1.0 O B:GLU449 4.0 31.1 1.0 C2 B:X3G701 4.1 35.8 1.0 CAX B:X3G701 4.1 32.5 1.0 CD1 B:LEU501 4.2 34.9 1.0 CAM B:X3G701 4.2 33.3 1.0 CG B:MET448 4.2 29.9 1.0 CG2 B:VAL433 4.4 33.9 1.0 CB B:VAL433 4.5 32.7 1.0 CBA B:X3G701 4.8 33.2 1.0 CA B:MET448 4.9 30.1 1.0 O B:ALA400 5.0 32.7 1.0 C B:MET448 5.0 30.4 1.0

S.J.Lee, J.S.Choi, B.G.Han, H.S.Kim, H.J.Song, J.Lee, S.Nam, S.H.Goh, J.H.Kim, J.S.Koh, B.I.Lee. Crystal Structures of Spleen Tyrosine Kinase in Complex with Novel Inhibitors: Structural Insights For Design of Anticancer Drugs Febs J. V. 283 3613 2016.
ISSN: ISSN 1742-464X
PubMed: 27504936
DOI: 10.1111/FEBS.13831