Fluorine in PDB 4d5h: Focal Adhesion Kinase Catalytic Domain

All present enzymatic activity of Focal Adhesion Kinase Catalytic Domain:
2.7.10.2;

The structure of Focal Adhesion Kinase Catalytic Domain, PDB code: 4d5h was solved by J.Le Coq, A.Lin, D.Lietha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.66 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.892, 123.587, 50.803, 90.00, 95.00, 90.00
R / Rfree (%)	18.144 / 20.503

The binding sites of Fluorine atom in the Focal Adhesion Kinase Catalytic Domain (pdb code 4d5h). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Focal Adhesion Kinase Catalytic Domain, PDB code: 4d5h:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Focal Adhesion Kinase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Focal Adhesion Kinase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:F1687 b:45.1 occ:0.75 FAC A:9RM1687 0.0 45.1 0.8 CAS A:9RM1687 1.4 44.1 0.8 FAE A:9RM1687 2.2 44.5 0.8 FAD A:9RM1687 2.2 49.2 0.8 CAP A:9RM1687 2.3 38.5 0.8 CAH A:9RM1687 2.7 38.1 0.8 OE1 A:GLU506 3.2 56.0 1.0 CD A:GLU506 3.2 48.9 1.0 O A:ILE428 3.3 35.5 1.0 CA A:GLY429 3.3 30.7 1.0 CG A:GLU506 3.3 41.6 1.0 CAI A:9RM1687 3.6 33.7 0.8 C A:ILE428 3.7 31.8 1.0 N A:GLY429 3.8 30.9 1.0 OE2 A:GLU506 3.8 54.8 1.0 CAF A:9RM1687 4.1 37.0 0.8 CB A:GLU506 4.3 35.3 1.0 N A:GLU506 4.3 28.5 1.0 C A:GLY429 4.4 30.3 1.0 N A:GLU430 4.6 33.4 1.0 CAO A:9RM1687 4.7 35.5 0.8 CA A:GLU506 4.9 30.1 1.0 CA A:ILE428 4.9 31.9 1.0 O A:HOH2037 4.9 40.0 1.0 CAG A:9RM1687 5.0 37.2 0.8 CB A:ILE428 5.0 32.6 1.0

Fluorine binding site 2 out of 3 in the Focal Adhesion Kinase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Focal Adhesion Kinase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:F1687 b:49.2 occ:0.75 FAD A:9RM1687 0.0 49.2 0.8 CAS A:9RM1687 1.4 44.1 0.8 FAE A:9RM1687 2.2 44.5 0.8 FAC A:9RM1687 2.2 45.1 0.8 CAP A:9RM1687 2.3 38.5 0.8 CAI A:9RM1687 2.9 33.7 0.8 CG1 A:ILE428 3.0 31.9 1.0 C A:ILE428 3.1 31.8 1.0 N A:GLY429 3.3 30.9 1.0 CB A:ILE428 3.3 32.6 1.0 O A:ILE428 3.3 35.5 1.0 CD1 A:ILE428 3.4 31.3 1.0 CAH A:9RM1687 3.4 38.1 0.8 O A:HOH2037 3.6 40.0 1.0 CA A:GLY429 3.6 30.7 1.0 CA A:ILE428 3.7 31.9 1.0 CAO A:9RM1687 4.2 35.5 0.8 CB A:VAL436 4.5 22.0 1.0 CG1 A:VAL436 4.5 20.9 1.0 CAF A:9RM1687 4.6 37.0 0.8 NAK A:9RM1687 4.6 36.0 0.8 C A:GLY429 4.6 30.3 1.0 N A:ILE428 4.7 30.5 1.0 CG2 A:ILE428 4.7 32.1 1.0 CAG A:9RM1687 4.9 37.2 0.8 O A:VAL436 4.9 24.3 1.0

Fluorine binding site 3 out of 3 in the Focal Adhesion Kinase Catalytic Domain


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Focal Adhesion Kinase Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:F1687 b:44.5 occ:0.75 FAE A:9RM1687 0.0 44.5 0.8 CAS A:9RM1687 1.4 44.1 0.8 FAC A:9RM1687 2.2 45.1 0.8 FAD A:9RM1687 2.2 49.2 0.8 CAP A:9RM1687 2.3 38.5 0.8 CAI A:9RM1687 2.7 33.7 0.8 O A:HOH2037 3.0 40.0 1.0 N A:GLU506 3.3 28.5 1.0 CAH A:9RM1687 3.4 38.1 0.8 CA A:GLY505 3.5 28.8 1.0 CG A:GLU506 3.5 41.6 1.0 C A:GLY505 3.6 28.4 1.0 CAO A:9RM1687 4.1 35.5 0.8 CD2 A:LEU553 4.1 25.8 1.0 CA A:GLU506 4.1 30.1 1.0 CB A:GLU506 4.2 35.3 1.0 CD A:GLU506 4.2 48.9 1.0 NAK A:9RM1687 4.3 36.0 0.8 O A:GLY505 4.5 24.9 1.0 CAF A:9RM1687 4.5 37.0 0.8 OE1 A:GLU506 4.6 56.0 1.0 O A:ILE428 4.7 35.5 1.0 N A:GLY505 4.7 28.6 1.0 CAG A:9RM1687 4.8 37.2 0.8 CD1 A:ILE428 4.8 31.3 1.0 CG1 A:ILE428 4.9 31.9 1.0 OE2 A:GLU506 4.9 54.8 1.0 C A:ILE428 5.0 31.8 1.0 NAL A:9RM1687 5.0 36.7 0.8

J.Zhou, A.Bronowska, J.Le Coq, D.Lietha, F.Grater. Allosteric Regulation of Focal Adhesion Kinase By PIP2 and Atp. Biophys.J. V. 108 698 2015.
ISSN: ISSN 0006-3495
PubMed: 25650936
DOI: 10.1016/J.BPJ.2014.11.3454