Bromine in PDB 5aol: Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine

The structure of Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine, PDB code: 5aol was solved by A.C.Joerger, H.Harbrecht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.42 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.910, 71.240, 105.020, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16.9

The structure of Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Zinc	(Zn)	2 atoms

The binding sites of Bromine atom in the Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine (pdb code 5aol). 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 Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine, PDB code: 5aol:

Bromine binding site 1 out of 1 in the Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of the P53 Cancer Mutant Y220C with Bound 3-Bromo-5- (Trifluoromethyl)Benzene-1,2-Diamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1293 b:18.2 occ:0.60 BR A:UFV1293 0.0 18.2 0.6 C1 A:UFV1293 1.9 14.6 0.6 O A:PRO219 2.7 14.5 0.4 N A:GLU221 2.8 22.1 0.4 C6 A:UFV1293 2.9 15.4 0.6 C2 A:UFV1293 2.9 14.1 0.6 N1 A:UFV1293 3.1 14.5 0.6 CA A:CYS220 3.1 18.9 0.4 C A:CYS220 3.4 20.7 0.4 C A:PRO219 3.6 14.7 0.4 N A:CYS220 3.8 16.5 0.4 CG A:GLU221 3.9 27.4 0.4 CA A:GLU221 3.9 23.9 0.4 CB A:GLU221 3.9 25.9 0.4 O A:PRO219 3.9 12.9 0.6 CD1 A:LEU145 3.9 16.5 1.0 CG2 A:VAL218 4.0 13.9 1.0 CA A:CYS220 4.0 13.4 0.6 O A:HOH2245 4.1 43.2 1.0 C5 A:UFV1293 4.2 15.9 0.6 C3 A:UFV1293 4.2 14.0 0.6 O A:HOH2224 4.2 23.6 1.0 CG2 A:VAL157 4.3 11.8 1.0 CD1 A:ILE232 4.3 15.2 0.5 CB A:CYS220 4.3 19.9 0.4 CG2 A:THR230 4.3 20.6 0.7 C A:PRO219 4.4 12.3 0.6 N A:CYS220 4.4 12.4 0.6 CG1 A:ILE232 4.4 14.2 0.5 CG2 A:THR230 4.4 16.3 0.3 O A:GLU221 4.4 24.1 0.4 CD A:GLU221 4.6 28.9 0.4 SG A:CYS220 4.6 14.0 0.6 OG1 A:THR230 4.6 18.4 0.3 O A:CYS220 4.7 21.1 0.4 SG A:CYS220 4.7 20.8 0.4 C A:GLU221 4.7 24.3 0.4 C4 A:UFV1293 4.7 15.3 0.6 CB A:CYS220 4.8 13.6 0.6 CB A:VAL157 4.8 9.2 1.0 N A:GLU221 4.9 16.0 0.6 OE1 A:GLU221 5.0 29.8 0.4 CA A:PRO219 5.0 13.4 0.4

A.C.Joerger, M.R.Bauer, R.Wilcken, M.G.J.Baud, H.Harbrecht, T.E.Exner, F.M.Boeckler, J.Spencer, A.R.Fersht. Exploiting Transient Protein States For the Design of Small-Molecule Stabilizers of Mutant P53. Structure V. 23 2246 2015.
ISSN: ISSN 0969-2126
PubMed: 26636255
DOI: 10.1016/J.STR.2015.10.016