Chlorine in PDB 4o7a: Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-409514

The structure of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-409514, PDB code: 4o7a was solved by S.W.Ember, J.-Y.Zhu, C.Watts, E.Schonbrunn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.98 / 1.34
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.199, 44.146, 78.383, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 17.4

The binding sites of Chlorine atom in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-409514 (pdb code 4o7a). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-409514, PDB code: 4o7a:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-409514


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 BRD4 in Complex with Sb-409514 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:17.7 occ:1.00 CL1 A:2RF201 0.0 17.7 1.0 C05 A:2RF201 1.7 17.7 1.0 C04 A:2RF201 2.7 17.2 1.0 C06 A:2RF201 2.7 19.8 1.0 H041 A:2RF201 2.8 20.5 1.0 H061 A:2RF201 2.8 23.7 1.0 HB A:ILE146 3.0 9.9 1.0 HD11 A:ILE146 3.1 13.0 1.0 HD13 A:ILE146 3.5 13.0 1.0 HA A:ILE146 3.5 9.6 1.0 SD A:MET149 3.5 8.2 1.0 CD1 A:ILE146 3.7 10.9 1.0 CB A:ILE146 3.8 8.3 1.0 HB3 A:ASP145 3.8 15.6 1.0 HH2 A:TRP81 3.9 13.5 1.0 HB2 A:ASP145 3.9 15.6 1.0 CA A:ILE146 3.9 8.1 1.0 C03 A:2RF201 4.0 18.0 1.0 N A:ILE146 4.0 8.6 1.0 HG2 A:PRO82 4.0 8.7 1.0 H A:ILE146 4.0 10.3 1.0 C01 A:2RF201 4.0 20.2 1.0 HG3 A:PRO82 4.0 8.7 1.0 O A:HOH320 4.1 13.1 1.0 HE2 A:MET149 4.1 10.9 1.0 CH2 A:TRP81 4.3 11.3 1.0 CG1 A:ILE146 4.3 10.3 1.0 CB A:ASP145 4.3 13.1 1.0 HZ2 A:TRP81 4.4 12.4 1.0 CG A:PRO82 4.4 7.3 1.0 CE A:MET149 4.5 9.1 1.0 HD12 A:ILE146 4.5 13.0 1.0 C02 A:2RF201 4.5 19.2 1.0 C A:ASP145 4.5 10.2 1.0 CZ2 A:TRP81 4.5 10.4 1.0 HB3 A:PRO82 4.5 9.1 1.0 H011 A:2RF201 4.8 24.1 1.0 HG12 A:ILE146 4.8 12.3 1.0 CB A:PRO82 5.0 7.6 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-409514


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 BRD4 in Complex with Sb-409514 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:19.2 occ:1.00 CL2 A:2RF201 0.0 19.2 1.0 C18 A:2RF201 1.7 16.2 1.0 C19 A:2RF201 2.7 13.5 1.0 C17 A:2RF201 2.7 16.3 1.0 H171 A:2RF201 2.8 19.5 1.0 O22 A:2RF201 2.9 12.6 1.0 HD22 A:ASN140 3.2 8.4 1.0 HD13 A:LEU94 3.2 13.4 1.0 HD12 A:LEU94 3.4 13.4 1.0 HD2 A:TYR139 3.6 8.1 1.0 OD1 A:ASN140 3.6 9.1 1.0 HE2 A:TYR139 3.7 10.1 1.0 CD1 A:LEU94 3.7 11.3 1.0 HG22 A:ILE146 3.8 10.3 1.0 H221 A:2RF201 3.8 15.1 1.0 HG12 A:ILE146 3.9 12.3 1.0 ND2 A:ASN140 3.9 7.1 1.0 C20 A:2RF201 4.0 14.5 1.0 C16 A:2RF201 4.0 15.7 1.0 H011 A:2RF201 4.1 24.1 1.0 HD11 A:LEU94 4.1 13.4 1.0 H021 A:2RF201 4.1 23.0 1.0 CD2 A:TYR139 4.1 6.8 1.0 C01 A:2RF201 4.2 20.2 1.0 CG A:ASN140 4.2 7.7 1.0 C02 A:2RF201 4.2 19.2 1.0 CE2 A:TYR139 4.2 8.5 1.0 HE1 A:TYR97 4.4 8.3 1.0 C21 A:2RF201 4.5 15.0 1.0 HD11 A:LEU92 4.6 13.4 1.0 HD21 A:ASN140 4.7 8.4 1.0 HD1 A:TYR97 4.7 8.4 1.0 CG2 A:ILE146 4.7 8.7 1.0 H201 A:2RF201 4.7 17.4 1.0 HD22 A:LEU94 4.7 14.7 1.0 CG1 A:ILE146 4.8 10.3 1.0 C06 A:2RF201 4.8 19.8 1.0 O A:HOH415 4.9 22.9 1.0 C03 A:2RF201 4.9 18.0 1.0 HB A:ILE146 4.9 9.9 1.0 HD23 A:LEU94 4.9 14.7 1.0 CE1 A:TYR97 4.9 7.0 1.0 HD11 A:ILE146 5.0 13.0 1.0 HG11 A:VAL87 5.0 11.1 1.0

S.W.Ember, J.Y.Zhu, S.H.Olesen, M.P.Martin, A.Becker, N.Berndt, G.I.Georg, E.Schonbrunn. Acetyl-Lysine Binding Site of Bromodomain-Containing Protein 4 (BRD4) Interacts with Diverse Kinase Inhibitors. Acs Chem.Biol. V. 9 1160 2014.
ISSN: ISSN 1554-8929
PubMed: 24568369
DOI: 10.1021/CB500072Z