Bromine in PDB 4xya: Crystal Structure of the First Bromodomain of Human BRD4 in Complex with A 2-Amine-9H-Purine Ligand

The structure of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with A 2-Amine-9H-Purine Ligand, PDB code: 4xya was solved by S.Picaud, F.Von Delft, A.M.Edwards, C.H.Arrowsmith, C.Bountra, P.Filippakopoulos, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.51 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.242, 44.373, 79.015, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 20.7

The binding sites of Bromine atom in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with A 2-Amine-9H-Purine Ligand (pdb code 4xya). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with A 2-Amine-9H-Purine Ligand, PDB code: 4xya:

Bromine binding site 1 out of 1 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with A 2-Amine-9H-Purine Ligand


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with A 2-Amine-9H-Purine Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:Br201 b:17.6 occ:1.00 BR A:43S201 0.0 17.6 1.0 C11 A:43S201 2.0 10.3 1.0 C12 A:43S201 2.8 10.0 1.0 C10 A:43S201 2.9 9.0 1.0 CZ3 A:TRP81 3.7 9.1 1.0 CD2 A:LEU92 4.0 10.6 1.0 CH2 A:TRP81 4.0 9.1 1.0 C9 A:43S201 4.2 10.5 1.0 C5 A:43S201 4.2 8.8 1.0 O A:HOH409 4.6 12.8 1.0 C6 A:43S201 4.7 8.3 1.0 CE3 A:TRP81 4.9 9.1 1.0

S.Picaud, M.Strocchia, S.Terracciano, G.Lauro, J.Mendez, D.L.Daniels, R.Riccio, G.Bifulco, I.Bruno, P.Filippakopoulos. The 9H-Purine Scaffold Reveals Induced-Fit Pocket Plasticity of the BRD9 Bromodomain. J.Med.Chem. 2015.
ISSN: ISSN 0022-2623
PubMed: 25703523
DOI: 10.1021/JM501893K