Fluorine in PDB 4o7f: Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527

The structure of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527, PDB code: 4o7f 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)	19.75 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.869, 59.464, 109.606, 90.00, 90.00, 90.00
R / Rfree (%)	14 / 19.4

The structure of Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527 (pdb code 4o7f). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527, PDB code: 4o7f:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527


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 Sb-251527 within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:10.9 occ:1.00 F33 A:2RQ201 0.0 10.9 1.0 C30 A:2RQ201 1.3 9.2 1.0 C29 A:2RQ201 2.4 8.7 1.0 C31 A:2RQ201 2.4 7.9 1.0 H291 A:2RQ201 2.6 10.5 1.0 H311 A:2RQ201 2.6 9.5 1.0 HD1 A:PHE83 2.9 8.0 1.0 O A:HOH308 3.0 8.0 1.0 HG3 A:MET132 3.2 7.5 1.0 HE1 A:PHE83 3.2 9.4 1.0 HG2 A:MET132 3.3 7.5 1.0 HB2 A:CYS136 3.4 10.5 1.0 CD1 A:PHE83 3.5 6.7 1.0 O A:MET132 3.6 7.7 1.0 CE1 A:PHE83 3.6 7.8 1.0 C32 A:2RQ201 3.6 6.2 1.0 C28 A:2RQ201 3.6 7.9 1.0 CG A:MET132 3.7 6.3 1.0 HG22 A:VAL87 4.2 8.5 1.0 C27 A:2RQ201 4.2 8.1 1.0 HG21 A:VAL87 4.2 8.5 1.0 HA A:PHE83 4.2 7.0 1.0 O A:MET105 4.3 6.9 1.0 CB A:CYS136 4.3 8.8 1.0 HG23 A:VAL87 4.3 8.5 1.0 H A:CYS136 4.4 5.8 1.0 HB2 A:ASN135 4.4 9.1 1.0 H281 A:2RQ201 4.4 9.5 1.0 H321 A:2RQ201 4.4 7.4 1.0 HA A:MET132 4.4 6.4 1.0 CG2 A:VAL87 4.5 7.1 1.0 C A:MET132 4.5 6.8 1.0 HH A:TYR97 4.5 12.7 1.0 CG A:PHE83 4.6 7.3 1.0 O A:HOH313 4.6 10.0 1.0 HA A:CYS136 4.7 9.4 1.0 N A:CYS136 4.8 4.9 1.0 SD A:MET132 4.8 7.0 1.0 OH A:TYR97 4.8 10.6 1.0 CA A:MET132 4.8 5.3 1.0 CB A:MET132 4.8 5.8 1.0 HA A:ASP106 4.9 6.6 1.0 CA A:CYS136 4.9 7.9 1.0 CZ A:PHE83 4.9 8.5 1.0 HB3 A:CYS136 4.9 10.5 1.0 HB3 A:PHE83 4.9 6.1 1.0 SG A:CYS136 5.0 8.0 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the First Bromodomain of Human BRD4 in Complex with Sb-251527


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 Sb-251527 within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:10.5 occ:1.00 F33 B:2RQ201 0.0 10.5 1.0 C30 B:2RQ201 1.3 7.6 1.0 C29 B:2RQ201 2.4 7.0 1.0 C31 B:2RQ201 2.4 6.2 1.0 H291 B:2RQ201 2.6 8.4 1.0 H311 B:2RQ201 2.6 7.5 1.0 HD1 B:PHE83 2.8 7.6 1.0 HG3 B:MET132 2.9 6.2 1.0 O B:HOH306 2.9 11.0 1.0 HG2 B:MET132 3.1 6.2 1.0 CG B:MET132 3.4 5.2 1.0 CD1 B:PHE83 3.5 6.3 1.0 HE1 B:PHE83 3.5 9.0 1.0 C32 B:2RQ201 3.7 6.2 1.0 C28 B:2RQ201 3.7 6.0 1.0 HB2 B:CYS136 3.8 7.8 1.0 O B:MET132 3.8 5.8 1.0 CE1 B:PHE83 3.8 7.5 1.0 O B:MET105 3.9 7.1 1.0 HA B:PHE83 4.0 7.1 1.0 C27 B:2RQ201 4.2 5.3 1.0 HA B:ASP106 4.2 6.9 1.0 HG21 B:VAL87 4.3 7.4 1.0 HG22 B:VAL87 4.3 7.4 1.0 HA B:MET132 4.3 4.7 1.0 SD B:MET132 4.4 7.3 1.0 H321 B:2RQ201 4.4 7.5 1.0 H281 B:2RQ201 4.4 7.2 1.0 C B:MET132 4.5 5.4 1.0 O B:HOH303 4.5 8.0 1.0 HG23 B:VAL87 4.5 7.4 1.0 CG B:PHE83 4.6 6.1 1.0 CG2 B:VAL87 4.6 6.1 1.0 CB B:MET132 4.6 3.5 1.0 HB3 B:PHE83 4.6 6.5 1.0 HB2 B:ASN135 4.6 5.8 1.0 CB B:CYS136 4.7 6.5 1.0 CA B:MET132 4.7 3.9 1.0 HH B:TYR97 4.7 11.8 1.0 H B:CYS136 4.7 7.8 1.0 HB3 B:ASP106 4.8 6.9 1.0 OH B:TYR97 4.8 9.8 1.0 CA B:PHE83 4.8 5.9 1.0 CB B:PHE83 4.9 5.4 1.0 O B:PRO82 4.9 6.1 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