Chlorine in PDB 3zxq: Crystal Structure of the Atp-Binding Domain of Mycobacterium Tuberculosis Dost

The structure of Crystal Structure of the Atp-Binding Domain of Mycobacterium Tuberculosis Dost, PDB code: 3zxq was solved by H.Y.Cho, H.J.Cho, B.S.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.83 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.914, 65.867, 72.704, 90.00, 90.00, 90.00
R / Rfree (%)	19.416 / 23.163

The binding sites of Chlorine atom in the Crystal Structure of the Atp-Binding Domain of Mycobacterium Tuberculosis Dost (pdb code 3zxq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Atp-Binding Domain of Mycobacterium Tuberculosis Dost, PDB code: 3zxq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Atp-Binding Domain of Mycobacterium Tuberculosis Dost


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 the Atp-Binding Domain of Mycobacterium Tuberculosis Dost within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1574 b:18.9 occ:1.00 OG A:SER480 3.1 17.3 1.0 O A:HOH2003 3.3 15.3 1.0 NH2 A:ARG454 3.3 10.2 1.0 CB A:SER480 3.5 16.8 1.0 N A:SER480 3.5 15.2 1.0 CA A:PRO478 3.5 12.4 1.0 C A:PRO478 3.8 12.9 1.0 N A:LEU479 3.8 13.0 1.0 CA A:SER480 4.1 16.2 1.0 CB A:PRO478 4.1 13.0 1.0 CZ A:ARG454 4.3 9.6 1.0 NH1 A:ARG454 4.3 13.2 1.0 O A:PRO478 4.4 13.0 1.0 O A:GLY477 4.6 12.3 1.0 C A:LEU479 4.6 14.4 1.0 CA A:LEU479 4.8 13.9 1.0 N A:PRO478 4.8 12.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Atp-Binding Domain of Mycobacterium Tuberculosis Dost


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 the Atp-Binding Domain of Mycobacterium Tuberculosis Dost within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1575 b:12.8 occ:1.00 O B:HOH2005 3.2 14.3 1.0 N B:ARG454 3.4 9.7 1.0 N B:LEU453 3.4 13.6 1.0 N B:SER480 3.6 11.8 1.0 CA B:SER480 3.7 12.6 1.0 C B:LEU479 3.7 11.9 1.0 CB B:LEU479 3.8 12.2 1.0 O B:HOH2003 3.8 14.6 1.0 O B:LEU479 3.9 12.1 1.0 C B:GLY452 3.9 15.4 1.0 CB B:ARG454 3.9 10.7 0.5 CA B:GLY452 3.9 17.6 1.0 CB B:ARG454 3.9 9.1 0.5 NH1 B:ARG454 4.1 22.8 0.5 CA B:LEU453 4.1 12.4 1.0 CB B:SER480 4.2 12.4 1.0 CB B:LEU453 4.2 12.4 1.0 C B:LEU453 4.2 10.9 1.0 CA B:ARG454 4.2 10.1 0.5 CA B:ARG454 4.2 9.1 0.5 CA B:LEU479 4.4 12.7 1.0 NH2 B:ARG454 4.4 2.1 0.5 O B:HOH2004 4.7 16.8 1.0 CZ B:ARG454 4.8 3.5 0.5 O B:GLY452 4.8 13.6 1.0 O B:HOH2026 4.9 26.7 1.0 NE B:ARG454 4.9 2.0 0.5 CD2 B:LEU479 5.0 13.3 1.0 C B:SER480 5.0 12.9 1.0 CG B:LEU479 5.0 13.5 1.0

H.Y.Cho, Y.H.Lee, Y.S.Bae, E.Kim, B.S.Kang. Activation of Atp Binding For the Autophosphorylation of Doss, A Mycobacterium Tuberculosis Histidine Kinase Lacking An Atp-Lid Motif. J.Biol.Chem. V. 288 12437 2013.
ISSN: ISSN 0021-9258
PubMed: 23486471
DOI: 10.1074/JBC.M112.442467