Chlorine in PDB 3nhv: Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F

The structure of Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F, PDB code: 3nhv was solved by F.Forouhar, H.Neely, J.Seetharaman, M.Mao, R.Xiao, C.Ciccosanti, D.Lee, J.K.Everett, R.Nair, T.B.Acton, B.Rost, G.T.Montelione, L.Tong, J.F.Hunt, Northeast Structural Genomics Consortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.85 / 2.50
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	145.873, 145.873, 145.873, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24.7

The binding sites of Chlorine atom in the Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F (pdb code 3nhv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F, PDB code: 3nhv:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:72.6 occ:1.00 NZ B:LYS128 3.1 57.2 1.0 NZ A:LYS128 3.4 63.2 1.0 NZ C:LYS128 3.6 80.6 1.0 CE B:LYS128 3.8 62.1 1.0 CE A:LYS128 4.1 48.2 1.0 CE C:LYS128 4.3 78.5 1.0 CZ A:PHE144 4.5 55.8 1.0 CD B:LYS128 4.8 49.3 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl201 b:42.6 occ:1.00 NZ C:LYS75 3.2 53.6 1.0 CE C:LYS75 4.5 45.6 1.0 CD C:LYS75 4.8 43.5 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl201 b:43.0 occ:1.00 N D:ALA57 3.4 36.2 1.0 OD1 D:ASP56 3.5 76.5 1.0 CG D:PRO72 3.6 35.6 1.0 CB D:ALA57 3.8 30.7 1.0 CB B:LYS44 4.0 61.0 1.0 CB D:PRO72 4.0 29.7 1.0 CA D:ASP56 4.2 38.0 1.0 CD1 B:TYR46 4.2 45.5 1.0 CB B:TYR46 4.3 47.1 1.0 CA D:ALA57 4.3 35.0 1.0 C D:ASP56 4.3 32.5 1.0 CG D:ASP56 4.4 60.3 1.0 CB D:ASP56 4.5 43.1 1.0 CG B:TYR46 4.5 43.3 1.0 CG B:LYS44 4.6 59.8 1.0 O B:LYS44 4.7 51.5 1.0 CA B:TYR46 4.7 53.6 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of BH2092 Protein From Bacillus Halodurans, Northeast Structural Genomics Consortium Target BHR228F within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl201 b:53.7 occ:0.50 NZ E:LYS128 3.2 59.7 1.0 CE E:LYS128 4.2 48.5 1.0

F.Forouhar, H.Neely, J.Seetharaman, M.Mao, R.Xiao, C.Ciccosanti, D.Lee, J.K.Everett, R.Nair, T.B.Acton, B.Rost, G.T.Montelione, L.Tong, J.F.Hunt. Northeast Structural Genomics Consortium Target BHR228F To Be Published 2010.