Bromine in PDB 7p5t: Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216

All present enzymatic activity of Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216:
1.14.15.28;

The structure of Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216, PDB code: 7p5t was solved by M.Snee, M.Kavanagh, R.Tunnicliffe, K.Mclean, C.Levy, A.Munro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	64.53 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.728, 65.717, 129.069, 90, 90, 90
R / Rfree (%)	13.7 / 16.2

The structure of Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216 also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Potassium	(K)	2 atoms

The binding sites of Bromine atom in the Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216 (pdb code 7p5t). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216, PDB code: 7p5t:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br403 b:18.9 occ:0.88 OG1 A:THR45 3.2 15.5 1.0 O A:HOH1018 3.4 22.7 1.0 ND1 A:HIS291 3.6 17.8 1.0 CB A:PRO32 3.8 17.7 1.0 CB A:THR45 3.9 14.2 1.0 CG2 A:THR45 4.0 15.5 1.0 CG A:PRO32 4.0 18.3 1.0 CE1 A:HIS291 4.1 18.1 1.0 CG A:HIS291 4.1 16.8 1.0 CB A:GLN47 4.2 18.5 1.0 CB A:HIS291 4.4 17.0 1.0 N A:ALA48 4.5 14.6 1.0 CG A:GLN47 4.6 23.4 1.0 CB A:ALA48 4.7 16.2 1.0 NE2 A:HIS291 4.8 18.3 1.0 CD2 A:HIS291 4.8 17.9 1.0

Bromine binding site 2 out of 3 in the Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br404 b:27.7 occ:0.66 O A:HOH1087 3.2 48.1 1.0 O A:HOH1052 3.2 54.3 1.0 N A:ASP79 3.3 19.5 1.0 O A:HOH819 3.6 36.9 1.0 O A:ASP79 3.7 20.6 1.0 CA A:MET78 3.8 18.9 1.0 CB A:MET78 3.9 20.1 1.0 C A:MET78 4.1 19.2 1.0 CB A:ALA82 4.1 24.6 1.0 CA A:ASP79 4.3 19.4 1.0 CG A:MET78 4.3 21.4 1.0 C A:ASP79 4.4 19.4 1.0 CB A:ASP79 4.4 19.9 1.0 CB A:ALA62 4.5 20.8 1.0 O A:HOH579 4.7 44.3 1.0 CE A:MET78 4.8 24.4 1.0 O A:ASP77 4.9 19.2 1.0 O A:HOH773 5.0 43.9 1.0

Bromine binding site 3 out of 3 in the Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br405 b:23.6 occ:0.59 O A:HOH907 2.4 28.3 1.0 O A:HOH559 3.1 33.6 1.0 NZ A:LYS102 3.2 27.6 1.0 N A:LEU201 3.3 23.7 1.0 NH2 A:ARG98 3.4 32.7 1.0 CA A:LEU201 3.6 20.9 1.0 CG A:MET141 3.7 20.2 1.0 CB A:LEU201 3.7 20.6 1.0 C A:ASP200 3.7 24.7 1.0 CB A:MET141 3.9 20.3 1.0 CE A:MET141 4.1 23.0 1.0 O A:ASP199 4.2 35.6 1.0 CA A:ASP200 4.2 28.4 1.0 CE A:LYS102 4.2 26.0 1.0 CA A:MET141 4.3 19.1 1.0 O A:MET141 4.4 19.6 1.0 CZ A:ARG98 4.4 32.7 1.0 O A:ASP200 4.4 24.6 1.0 CD1 A:LEU201 4.4 20.4 1.0 O A:HOH870 4.5 47.5 1.0 NE A:ARG98 4.5 32.5 1.0 O A:HOH783 4.5 32.9 1.0 SD A:MET141 4.6 21.8 1.0 CG A:LEU201 4.7 20.0 1.0 C A:MET141 4.8 19.1 1.0

M.Kavanagh, A.Coyne. Structure of CYP142 From Mycobacterium Tuberculosis in Complex with Inhibitor MEK216 To Be Published.