Chlorine in PDB 2yek: Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet)

The structure of Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet), PDB code: 2yek was solved by C.W.Chung, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.96 / 1.98
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	116.243, 55.639, 66.231, 90.00, 93.63, 90.00
R / Rfree (%)	15.546 / 20.079

The binding sites of Chlorine atom in the Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet) (pdb code 2yek). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet), PDB code: 2yek:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1188 b:47.5 occ:1.00 CL A:EAM1188 0.0 47.5 1.0 C10 A:EAM1188 1.7 39.4 1.0 C9 A:EAM1188 2.7 34.3 1.0 C11 A:EAM1188 2.7 36.0 1.0 C8 A:EAM1188 3.9 31.9 1.0 C12 A:EAM1188 3.9 30.7 1.0 O A:HOH2095 4.1 50.6 1.0 O A:HOH2127 4.3 24.5 1.0 CB A:ASP161 4.3 26.3 1.0 C7 A:EAM1188 4.4 29.8 1.0 OD2 A:ASP161 4.5 33.9 1.0 CH2 A:TRP97 4.6 29.7 1.0 CZ2 A:TRP97 4.7 28.2 1.0 SD A:MET165 4.8 24.6 1.0 CG A:ASP161 4.9 28.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1183 b:36.0 occ:1.00 CL B:EAM1183 0.0 36.0 1.0 C10 B:EAM1183 1.7 31.4 1.0 C9 B:EAM1183 2.7 30.4 1.0 C11 B:EAM1183 2.7 30.3 1.0 O B:HOH2071 3.8 38.4 1.0 C8 B:EAM1183 3.9 29.8 1.0 C12 B:EAM1183 4.0 26.9 1.0 CB B:ASP161 4.0 27.8 1.0 O B:HOH2110 4.2 16.7 1.0 SD B:MET165 4.4 26.2 1.0 OD2 B:ASP161 4.4 31.2 1.0 CZ2 B:TRP97 4.4 28.4 1.0 C7 B:EAM1183 4.5 26.8 1.0 O B:HOH2108 4.5 27.8 1.0 CH2 B:TRP97 4.6 28.5 1.0 CG B:ASP161 4.7 28.9 1.0 N B:ILE162 4.9 23.1 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the First Bromodomain of Human BRD2 with the Inhibitor GSK525762 (Ibet) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1183 b:38.5 occ:1.00 CL C:EAM1183 0.0 38.5 1.0 C10 C:EAM1183 1.7 37.9 1.0 C9 C:EAM1183 2.7 34.4 1.0 C11 C:EAM1183 2.7 35.8 1.0 CB C:ASP161 3.7 36.8 1.0 CG A:PRO181 3.7 42.2 1.0 CB A:ASN77 3.8 32.5 1.0 OD2 C:ASP161 3.9 41.2 1.0 C8 C:EAM1183 4.0 31.2 1.0 C12 C:EAM1183 4.0 34.5 1.0 CZ2 C:TRP97 4.0 26.7 1.0 O A:ASN77 4.1 30.5 1.0 CG C:ASP161 4.2 38.8 1.0 CH2 C:TRP97 4.2 25.3 1.0 SD C:MET165 4.3 32.1 1.0 CA A:ASN77 4.4 32.5 1.0 CB A:PRO181 4.4 43.9 1.0 O C:HOH2103 4.5 28.2 1.0 C7 C:EAM1183 4.5 31.5 1.0 C A:ASN77 4.6 31.8 1.0 O C:HOH2105 4.6 26.8 1.0 CD A:PRO181 4.9 40.2 1.0 CG A:ASN77 5.0 34.7 1.0

C.W.Chung, H.Coste, J.H.White, O.Mirguet, J.Wilde, R.L.Gosmini, C.Delves, S.M.Magny, R.Woodward, S.A.Hughes, E.V.Boursier, H.Flynn, A.M.Bouillot, P.Bamborough, J.M.Brusq, F.J.Gellibert, E.J.Jones, A.M.Riou, P.Homes, S.L.Martin, I.J.Uings, J.Toum, C.A.Clement, A.B.Boullay, R.L.Grimley, F.M.Blandel, R.K.Prinjha, K.Lee, J.Kirilovsky, E.Nicodeme. Discovery and Characterization of Small Molecule Inhibitors of the Bet Family Bromodomains. J.Med.Chem. V. 54 3827 2011.
ISSN: ISSN 0022-2623
PubMed: 21568322
DOI: 10.1021/JM200108T