Bromine in PDB 7zsr: Purine Nucleoside Phosphorylase in Complex with Js-379

All present enzymatic activity of Purine Nucleoside Phosphorylase in Complex with Js-379:
2.4.2.1;

The structure of Purine Nucleoside Phosphorylase in Complex with Js-379, PDB code: 7zsr was solved by S.Djukic, P.Pachl, P.Rezacova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.92 / 1.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.528, 84.54, 93.879, 90, 94.47, 90
R / Rfree (%)	18.9 / 25.3

The binding sites of Bromine atom in the Purine Nucleoside Phosphorylase in Complex with Js-379 (pdb code 7zsr). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Purine Nucleoside Phosphorylase in Complex with Js-379, PDB code: 7zsr:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Purine Nucleoside Phosphorylase in Complex with Js-379


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Purine Nucleoside Phosphorylase in Complex with Js-379 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br301 b:53.4 occ:0.95 BR1 A:JSI301 0.0 53.4 0.9 C10 A:JSI301 1.9 48.2 0.9 C9 A:JSI301 2.8 46.8 0.9 C11 A:JSI301 2.9 41.5 0.9 CD1 A:LEU247 3.4 39.8 1.0 CE1 A:HIS243 4.0 36.7 1.0 O A:HOH470 4.0 40.2 1.0 CE2 B:PHE153 4.1 43.7 1.0 OG A:SER36 4.1 59.1 1.0 C8 A:JSI301 4.1 43.0 0.9 C12 A:JSI301 4.2 38.7 0.9 CB A:SER36 4.2 54.5 1.0 CZ B:PHE153 4.2 38.0 1.0 CD2 B:PHE153 4.5 46.7 1.0 NE2 A:HIS243 4.5 35.7 1.0 C7 A:JSI301 4.7 37.8 0.9 O A:HOH454 4.7 40.9 1.0 CE1 B:PHE153 4.7 45.0 1.0 O A:HOH442 4.8 33.8 1.0 CG A:LEU247 4.9 41.4 1.0

Bromine binding site 2 out of 3 in the Purine Nucleoside Phosphorylase in Complex with Js-379


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Purine Nucleoside Phosphorylase in Complex with Js-379 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br301 b:54.5 occ:0.95 BR1 B:JSI301 0.0 54.5 0.9 C10 B:JSI301 1.9 50.0 0.9 C11 B:JSI301 2.8 48.5 0.9 C9 B:JSI301 2.9 49.1 0.9 CD2 C:PHE153 3.4 88.6 1.0 CB C:PHE153 3.5 77.6 1.0 CG C:PHE153 3.8 88.3 1.0 OH B:TYR92 3.9 43.0 1.0 CZ B:TYR92 4.0 39.2 1.0 C12 B:JSI301 4.1 46.5 0.9 CA C:GLY151 4.2 57.9 1.0 C8 B:JSI301 4.2 44.6 0.9 O B:PRO186 4.2 30.3 1.0 CE2 B:TYR92 4.3 36.0 1.0 SD B:MET207 4.4 36.5 1.0 CB B:PRO186 4.4 28.7 1.0 CE2 C:PHE153 4.4 92.7 1.0 CE1 B:TYR92 4.5 39.2 1.0 CA C:PHE153 4.6 68.3 1.0 C C:GLY151 4.7 65.3 1.0 C7 B:JSI301 4.7 43.0 0.9 O C:GLY151 4.9 60.3 1.0 CA B:PRO186 4.9 29.5 1.0 N C:PHE153 4.9 62.1 1.0 CD2 B:TYR92 4.9 34.9 1.0 C B:PRO186 5.0 28.3 1.0

Bromine binding site 3 out of 3 in the Purine Nucleoside Phosphorylase in Complex with Js-379


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Purine Nucleoside Phosphorylase in Complex with Js-379 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br301 b:40.9 occ:0.95 BR1 C:JSI301 0.0 40.9 0.9 C10 C:JSI301 1.9 40.2 0.9 C9 C:JSI301 2.8 41.4 0.9 C11 C:JSI301 2.9 38.1 0.9 O C:HOH472 3.5 44.3 1.0 CE2 A:PHE153 3.6 38.9 1.0 CE1 C:HIS243 3.7 41.7 1.0 CZ A:PHE153 3.7 37.5 1.0 CD2 C:LEU247 3.9 46.3 1.0 CB C:SER36 3.9 55.8 1.0 OG C:SER36 4.0 54.1 1.0 NE2 C:HIS243 4.0 41.8 1.0 C8 C:JSI301 4.1 36.7 0.9 C12 C:JSI301 4.2 38.9 0.9 CD2 A:PHE153 4.4 39.0 1.0 CE1 A:PHE153 4.4 38.3 1.0 C7 C:JSI301 4.7 35.9 0.9 ND1 C:HIS243 4.9 36.2 1.0 CG C:LEU247 4.9 43.7 1.0 O C:HOH405 5.0 36.3 1.0 CG A:PHE153 5.0 37.8 1.0 CD1 A:PHE153 5.0 38.9 1.0

J.Skacel, S.Djukic. Design, Synthesis, Biological Evaluation, and Crystallographic Study of Novel Pnp Inhibitors To Be Published.