Sodium in PDB 7lh8: Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Inhibitor Jj-II-131

The structure of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Inhibitor Jj-II-131, PDB code: 7lh8 was solved by E.Schonbrunn, A.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.19 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.88, 49.43, 53.13, 90, 90, 90
R / Rfree (%)	17.3 / 21.2

The binding sites of Sodium atom in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Inhibitor Jj-II-131 (pdb code 7lh8). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Inhibitor Jj-II-131, PDB code: 7lh8:

Sodium binding site 1 out of 1 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Inhibitor Jj-II-131


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Inhibitor Jj-II-131 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na208 b:20.8 occ:1.00 OG1 A:THR60 3.1 22.8 1.0 N A:ALA122 3.2 15.7 1.0 CA A:ASN121 3.6 15.3 1.0 CB A:ASN121 3.6 17.0 1.0 CG2 A:THR60 3.7 27.5 1.0 CB A:THR60 3.7 24.0 1.0 C A:ASN121 3.9 16.7 1.0 NH2 A:ARG58 3.9 28.0 1.0 CB A:ALA122 3.9 18.6 1.0 CB A:GLN62 4.0 28.4 1.0 OE1 A:GLN62 4.0 49.2 1.0 O A:HOH358 4.1 39.3 1.0 CA A:ALA122 4.1 16.9 1.0 OE1 A:GLN123 4.2 17.1 0.5 CD1 A:LEU63 4.6 16.6 1.0 CG A:GLN62 4.6 31.4 1.0 CG A:LEU63 4.6 18.0 1.0 O A:TRP120 4.6 16.6 1.0 CD A:GLN62 4.7 50.8 1.0 N A:LEU63 4.9 22.1 1.0 N A:ASN121 4.9 14.5 1.0 CZ A:ARG58 4.9 23.8 1.0 CG A:ASN121 5.0 15.4 1.0

E.Schonbrunn, A.Chan. Exploring the Za Channel of Bet Bromodomains: Design, Synthesis, and Evaluation of Dihydropyridine Analogs To Be Published.