Bromine in PDB 8je7: Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)

The structure of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95), PDB code: 8je7 was solved by R.Goswami, Y.Manickam, J.Chhibber-Goel, K.Harlos, A.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.81 / 2.14
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.675, 113.712, 123.999, 90, 90, 90
R / Rfree (%)	18 / 22.8

The structure of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Chlorine	(Cl)	6 atoms

The binding sites of Bromine atom in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) (pdb code 8je7). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 6 binding sites of Bromine where determined in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95), PDB code: 8je7:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6;

Bromine binding site 1 out of 6 in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1801 b:145.8 occ:0.93 BR1 A:HFG1801 0.0 145.8 0.9 C7 A:HFG1801 1.9 83.9 0.9 C8 A:HFG1801 2.8 52.3 0.9 C6 A:HFG1801 2.9 59.6 0.9 O A:HOH1964 3.3 60.3 1.0 CL1 A:HFG1801 3.3 52.3 0.9 CG1 A:VAL1308 3.5 72.7 1.0 N A:GLU1307 3.7 75.1 1.0 O A:HOH1911 3.7 53.8 0.4 CB A:PRO1327 3.9 36.5 1.0 C A:GLU1307 3.9 60.8 1.0 CB A:PRO1306 3.9 88.2 1.0 N A:VAL1308 4.0 52.8 1.0 O A:GLU1307 4.1 65.5 1.0 C9 A:HFG1801 4.1 47.8 0.9 C A:PRO1306 4.2 80.5 1.0 CG A:PRO1327 4.2 40.3 1.0 C5 A:HFG1801 4.2 50.3 0.9 CA A:GLU1307 4.3 69.8 1.0 CA A:PRO1306 4.4 89.7 1.0 CA A:VAL1308 4.4 58.7 1.0 CB A:VAL1308 4.5 65.6 1.0 O A:HOH1911 4.6 57.5 0.6 O A:HOH2036 4.6 72.5 1.0 C10 A:HFG1801 4.7 50.1 0.9 CB A:GLU1307 4.8 71.9 1.0 CG A:ARG1359 4.8 43.4 1.0 O A:PRO1306 4.9 69.7 1.0

Bromine binding site 2 out of 6 in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1803 b:48.6 occ:0.44 O7' A:HFG1801 3.1 43.3 0.9 NH1 A:ARG1359 3.2 47.5 1.0 NH2 A:ARG1359 3.2 41.7 1.0 C19 A:JE61802 3.3 48.8 0.9 O4' A:HFG1801 3.5 46.2 0.9 C21 A:HFG1801 3.5 50.1 0.9 C2 A:HFG1801 3.6 43.3 0.9 C39 A:HFG1801 3.6 41.5 0.9 C1' A:HFG1801 3.7 45.7 0.9 CZ A:ARG1359 3.7 53.2 1.0 C18 A:JE61802 3.7 44.3 0.9 C15 A:JE61802 4.0 41.5 0.9 N3 A:HFG1801 4.1 41.7 0.9 C3' A:HFG1801 4.3 41.5 0.9 C14 A:JE61802 4.4 43.9 0.9 CZ3 A:TRP1376 4.4 45.8 1.0 N1 A:HFG1801 4.5 47.4 0.9 C16 A:JE61802 4.5 43.8 0.9 C2' A:HFG1801 4.5 39.0 0.9 C20 A:JE61802 4.6 38.2 0.9 C4' A:HFG1801 4.8 42.9 0.9 CH2 A:TRP1376 4.9 45.8 1.0

Bromine binding site 3 out of 6 in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1804 b:108.7 occ:0.76 CD1 A:PHE1423 3.9 56.2 1.0 C1' A:HFG1801 3.9 45.7 0.9 C2 A:HFG1801 4.3 43.3 0.9 N3 A:HFG1801 4.3 41.7 0.9 CA A:PHE1423 4.4 52.1 1.0 CB A:PHE1423 4.7 56.8 1.0 CE1 A:PHE1423 4.7 55.7 1.0 CG A:PHE1423 4.7 58.3 1.0

Bromine binding site 4 out of 6 in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1801 b:128.6 occ:0.87 BR1 B:HFG1801 0.0 128.6 0.9 C7 B:HFG1801 1.9 63.8 0.9 C8 B:HFG1801 2.8 42.8 0.9 C6 B:HFG1801 2.9 39.4 0.9 O B:HOH1959 3.0 70.2 1.0 CL1 B:HFG1801 3.3 44.7 0.9 O B:HOH2055 3.3 47.0 0.8 CG1 B:VAL1308 3.6 50.8 1.0 C B:GLU1307 3.7 58.4 1.0 O B:GLU1307 3.7 63.3 1.0 N B:GLU1307 3.7 58.5 1.0 CB B:PRO1327 3.9 41.6 1.0 O B:HOH2098 3.9 65.9 1.0 N B:VAL1308 4.0 46.2 1.0 CG B:PRO1327 4.1 36.6 1.0 CA B:GLU1307 4.1 58.8 1.0 C9 B:HFG1801 4.1 37.3 0.9 C5 B:HFG1801 4.2 37.7 0.9 O B:HOH1998 4.2 50.5 1.0 CB B:PRO1306 4.3 72.8 1.0 C B:PRO1306 4.4 66.7 1.0 CB B:GLU1307 4.4 64.3 1.0 CA B:VAL1308 4.5 51.6 1.0 CA B:PRO1306 4.6 68.4 1.0 C10 B:HFG1801 4.7 37.6 0.9 CB B:VAL1308 4.7 53.6 1.0

Bromine binding site 5 out of 6 in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1803 b:59.9 occ:0.77 O7' B:HFG1801 3.1 32.8 0.9 NH1 B:ARG1359 3.3 43.9 1.0 NH2 B:ARG1359 3.4 43.9 1.0 C19 B:JE61802 3.5 37.4 0.9 O4' B:HFG1801 3.5 33.2 0.9 C21 B:HFG1801 3.6 42.9 0.9 C39 B:HFG1801 3.7 28.0 0.9 C18 B:JE61802 3.7 35.6 0.9 C2 B:HFG1801 3.8 32.2 0.9 CZ B:ARG1359 3.8 46.6 1.0 C1' B:HFG1801 3.8 39.8 0.9 C15 B:JE61802 3.8 29.0 0.9 O B:HOH2097 4.1 63.4 1.0 C14 B:JE61802 4.1 30.5 0.9 N3 B:HFG1801 4.2 35.9 0.9 CZ3 B:TRP1376 4.4 34.1 1.0 C16 B:JE61802 4.4 36.5 0.9 C3' B:HFG1801 4.4 38.4 0.9 C2' B:HFG1801 4.6 37.2 0.9 N1 B:HFG1801 4.6 34.7 0.9 C20 B:JE61802 4.7 33.4 0.9 C4' B:HFG1801 4.8 27.5 0.9 CH2 B:TRP1376 4.8 39.5 1.0

Bromine binding site 6 out of 6 in the Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Crystal Structure of Anopheles Culicifacies Prolyl-Trna Synthetase (Acprs) in Complex with Two Inhibitors (Halofuginone and L95) within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1804 b:102.2 occ:0.73 O B:HOH2011 3.5 58.7 1.0 C1' B:HFG1801 3.8 39.8 0.9 O B:HOH2073 3.9 60.2 0.9 CD1 B:PHE1423 4.0 36.5 1.0 O B:HOH2034 4.0 53.1 1.0 N3 B:HFG1801 4.3 35.9 0.9 C2 B:HFG1801 4.3 32.2 0.9 CA B:PHE1423 4.3 38.2 1.0 O B:HOH2097 4.4 63.4 1.0 CB B:PHE1423 4.6 44.7 1.0 CG B:PHE1423 4.6 42.0 1.0 CE1 B:PHE1423 4.7 40.6 1.0 N B:PHE1423 5.0 40.7 1.0

R.Goswami, J.Chhibber-Goel, Y.Manickam, S.Gupta, K.Harlos, B.Laleu, A.Sharma. Targeting Prolyl-Trna Synthetase of Anopheles Culicifacies For the Development of New Larvicide To Be Published.