Bromine in PDB 4qox: Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500

All present enzymatic activity of Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500:
2.7.11.1;

The structure of Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500, PDB code: 4qox was solved by A.K.Wernimont, J.R.Walker, A.Hutchinson, A.Seitova, H.He, P.Loppnau, M.Neculai, M.Amani, Y.H.Lin, M.Ravichandran, C.H.Arrowsmith, A.M.Edwards, C.Bountra, R.Hui, D.V.Lovato, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.56 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.289, 75.967, 92.688, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 26.6

The structure of Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500 also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Bromine atom in the Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500 (pdb code 4qox). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500, PDB code: 4qox:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500


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 CDPK4 From Plasmodium Falciparum, PF3D7_0717500 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br602 b:85.8 occ:0.37 BRAV A:DXR602 0.0 85.8 0.4 CAS A:DXR602 1.5 68.9 0.5 CAR A:DXR602 1.9 67.6 0.4 CAT A:DXR602 2.1 60.4 0.5 CAR A:DXR602 2.7 66.4 0.5 CAQ A:DXR602 2.8 59.3 0.4 CAS A:DXR602 2.8 82.1 0.4 CAU A:DXR602 3.4 56.4 0.5 BRAV A:DXR602 3.6 0.1 0.5 CB A:LEU145 3.6 41.1 1.0 SD A:MET131 3.6 66.7 1.0 CD1 A:LEU145 3.8 52.4 1.0 CAQ A:DXR602 3.8 57.7 0.5 CE A:MET131 4.1 0.1 1.0 CAP A:DXR602 4.1 55.0 0.5 CAP A:DXR602 4.1 54.7 0.4 CAT A:DXR602 4.1 86.2 0.4 CD1 A:LEU133 4.2 47.9 1.0 CG A:LEU145 4.3 47.2 1.0 CB A:LYS99 4.4 35.9 1.0 CD2 A:LEU218 4.5 75.2 1.0 CB A:SER147 4.5 30.6 1.0 CD1 A:LEU218 4.6 67.1 1.0 CAU A:DXR602 4.7 63.6 0.4 CD A:LYS99 4.7 43.0 1.0 O A:LEU145 4.7 46.1 1.0 C A:LEU145 4.8 41.1 1.0 CA A:LEU145 4.8 36.8 1.0 OD1 A:ASP215 4.8 57.1 1.0 CE A:LYS99 5.0 46.5 1.0 CD2 A:LEU145 5.0 53.3 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500


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 CDPK4 From Plasmodium Falciparum, PF3D7_0717500 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br602 b:0.1 occ:0.51 BRAV A:DXR602 0.0 0.1 0.5 CAS A:DXR602 0.9 82.1 0.4 CAT A:DXR602 1.3 86.2 0.4 CAR A:DXR602 1.9 66.4 0.5 CAR A:DXR602 2.3 67.6 0.4 CAU A:DXR602 2.7 63.6 0.4 CAS A:DXR602 2.8 68.9 0.5 CAQ A:DXR602 2.8 57.7 0.5 O A:ALA97 3.0 24.8 1.0 O A:LEU145 3.1 46.1 1.0 N A:LYS99 3.1 35.6 1.0 CAQ A:DXR602 3.3 59.3 0.4 CAP A:DXR602 3.4 54.7 0.4 CB A:SER147 3.5 30.6 1.0 C A:ALA97 3.6 25.0 1.0 BRAV A:DXR602 3.6 85.8 0.4 CB A:LYS99 3.6 35.9 1.0 C A:ILE98 3.8 36.1 1.0 CA A:ILE98 3.8 35.6 1.0 N A:SER147 3.8 25.2 1.0 N A:ILE98 3.9 27.2 1.0 CA A:LYS99 3.9 40.4 1.0 C A:LEU145 4.0 41.1 1.0 CAT A:DXR602 4.1 60.4 0.5 CAP A:DXR602 4.1 55.0 0.5 CA A:SER147 4.3 37.2 1.0 CB A:ALA97 4.3 24.5 1.0 C A:VAL146 4.5 36.4 1.0 CA A:ALA97 4.6 29.5 1.0 CAU A:DXR602 4.6 56.4 0.5 CB A:LEU145 4.6 41.1 1.0 CA A:VAL146 4.7 32.0 1.0 N A:VAL146 4.7 45.3 1.0 O A:ILE98 4.8 39.0 1.0 CG1 A:VAL84 4.8 41.7 1.0 CAO A:DXR602 4.8 52.0 0.4 NAG A:DXR602 4.9 46.5 0.5 CA A:LEU145 4.9 36.8 1.0

A.K.Wernimont, J.R.Walker, A.Hutchinson, A.Seitova, H.He, P.Loppnau, M.Neculai, M.Amani, Y.H.Lin, M.Ravichandran, C.H.Arrowsmith, A.M.Edwards, C.Bountra, R.Hui, D.V.Lovato. Crystal Structure of CDPK4 From Plasmodium Falciparum, PF3D7_0717500 To Be Published.