Fluorine in PDB 6u0d: Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590

The structure of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590, PDB code: 6u0d was solved by P.G.Leonard, S.Joseph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.95 / 1.43
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.470, 42.380, 80.290, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 22.3

The binding sites of Fluorine atom in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590 (pdb code 6u0d). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590, PDB code: 6u0d:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590


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 the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590 within 5.0Å range: probe atom residue distance (Å) B Occ A:F202 b:39.6 occ:1.00 F33 A:POJ202 0.0 39.6 1.0 C32 A:POJ202 1.3 30.6 1.0 F35 A:POJ202 2.1 32.6 1.0 F34 A:POJ202 2.1 38.5 1.0 C02 A:POJ202 2.4 26.1 1.0 NZ A:LYS155 2.8 40.5 1.0 C01 A:POJ202 2.9 29.3 1.0 CG A:LYS155 3.1 18.9 1.0 O A:HOH370 3.5 25.0 1.0 C03 A:POJ202 3.6 23.9 1.0 CD A:LYS155 3.6 26.8 1.0 CE A:LYS155 3.7 35.6 1.0 C A:LYS155 3.7 14.9 1.0 N A:LEU156 3.7 14.6 1.0 O A:LYS155 3.8 16.5 1.0 CB A:LYS155 3.8 15.6 1.0 CA A:LEU156 3.9 17.5 1.0 C06 A:POJ202 4.3 22.1 1.0 CA A:LYS155 4.4 14.6 1.0 CB A:LEU156 4.6 16.6 1.0 C04 A:POJ202 4.8 25.3 1.0 O A:HOH333 4.8 21.9 1.0 CB A:GLN159 4.9 16.5 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590


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 the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590 within 5.0Å range: probe atom residue distance (Å) B Occ A:F202 b:38.5 occ:1.00 F34 A:POJ202 0.0 38.5 1.0 C32 A:POJ202 1.3 30.6 1.0 F35 A:POJ202 2.1 32.6 1.0 F33 A:POJ202 2.1 39.6 1.0 C02 A:POJ202 2.5 26.1 1.0 NZ A:LYS155 2.7 40.5 1.0 C01 A:POJ202 3.2 29.3 1.0 C03 A:POJ202 3.5 23.9 1.0 CE A:LYS155 4.0 35.6 1.0 C06 A:POJ202 4.5 22.1 1.0 CG A:LYS155 4.5 18.9 1.0 CD A:LYS155 4.7 26.8 1.0 C04 A:POJ202 4.7 25.3 1.0 O A:HOH484 4.9 32.8 1.0 CG A:GLN159 5.0 21.6 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with the Inhibitor ZL0590 within 5.0Å range: probe atom residue distance (Å) B Occ A:F202 b:32.6 occ:1.00 F35 A:POJ202 0.0 32.6 1.0 C32 A:POJ202 1.3 30.6 1.0 F33 A:POJ202 2.1 39.6 1.0 F34 A:POJ202 2.1 38.5 1.0 C02 A:POJ202 2.4 26.1 1.0 C03 A:POJ202 2.9 23.9 1.0 CB A:GLN159 3.1 16.5 1.0 CG A:GLN159 3.4 21.6 1.0 O A:LYS155 3.5 16.5 1.0 C01 A:POJ202 3.7 29.3 1.0 NZ A:LYS155 3.9 40.5 1.0 O A:HOH333 3.9 21.9 1.0 CG A:LYS155 4.0 18.9 1.0 C A:LYS155 4.1 14.9 1.0 CA A:LEU156 4.2 17.5 1.0 C04 A:POJ202 4.3 25.3 1.0 CD A:GLN159 4.3 25.4 1.0 N A:LEU156 4.4 14.6 1.0 O A:HOH484 4.4 32.8 1.0 OE1 A:GLN159 4.5 27.4 1.0 CA A:GLN159 4.5 20.0 1.0 CE A:LYS155 4.6 35.6 1.0 N A:GLN159 4.8 17.3 1.0 C06 A:POJ202 4.8 22.1 1.0 CD A:LYS155 4.9 26.8 1.0 O A:LEU156 4.9 16.1 1.0 CB A:LYS155 5.0 15.6 1.0

Z.Liu, H.Chen, P.Wang, Y.Li, E.A.Wold, P.G.Leonard, S.Joseph, A.R.Brasier, B.Tian, J.Zhou. Identification of A Bromodomain-Containing Protein 4 (BRD4) BD1 Domain-Selective Inhibitor with A Distinguished New Binding Site To Be Published.