Zinc in PDB 3zxo: Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss

All present enzymatic activity of Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss:
2.7.13.3;

The structure of Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss, PDB code: 3zxo 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)	46.08 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	53.186, 53.186, 184.608, 90.00, 90.00, 90.00
R / Rfree (%)	18.58 / 23.585

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

Zinc binding site 1 out of 2 in the Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1579 b:14.4 occ:1.00 OD2 A:ASP529 1.8 13.8 1.0 NE2 A:HIS507 1.9 15.6 1.0 O A:HOH2062 2.0 12.4 1.0 OE2 A:GLU537 2.0 13.9 1.0 CD A:GLU537 2.6 15.4 1.0 OE1 A:GLU537 2.7 14.9 1.0 CG A:ASP529 2.8 14.4 1.0 CD2 A:HIS507 2.8 17.0 1.0 CE1 A:HIS507 3.0 20.9 1.0 OD1 A:ASP529 3.1 11.4 1.0 O A:VAL505 3.6 14.3 1.0 O A:HOH2070 3.9 11.0 1.0 O A:HOH2084 3.9 23.7 1.0 N A:VAL505 4.0 14.9 1.0 CG A:HIS507 4.0 19.7 1.0 ND1 A:HIS507 4.1 20.0 1.0 CG A:GLU537 4.1 14.3 1.0 CB A:ASP529 4.1 14.5 1.0 CZ A:PHE538 4.3 15.2 1.0 CE2 A:PHE538 4.3 13.4 1.0 CB A:ALA504 4.4 11.7 1.0 CA A:ALA504 4.5 13.4 1.0 C A:VAL505 4.6 16.5 1.0 CG2 A:VAL505 4.7 16.6 1.0 C A:ALA504 4.7 13.4 1.0 CA A:GLY531 4.8 16.9 1.0 CA A:VAL505 4.9 15.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Mutant Atp-Binding Domain of Mycobacterium Tuberculosis Doss within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1578 b:12.8 occ:1.00 OD2 B:ASP529 1.9 13.0 1.0 O B:HOH2042 1.9 12.9 1.0 NE2 B:HIS507 2.0 15.9 1.0 OE2 B:GLU537 2.0 11.5 1.0 OE1 B:GLU537 2.5 13.3 1.0 CD B:GLU537 2.6 11.0 1.0 CG B:ASP529 2.8 14.7 1.0 CE1 B:HIS507 3.0 19.1 1.0 CD2 B:HIS507 3.0 14.7 1.0 OD1 B:ASP529 3.1 11.0 1.0 O B:VAL505 3.6 15.5 1.0 O B:HOH2052 3.8 10.3 1.0 N B:VAL505 4.0 15.3 1.0 CG B:GLU537 4.1 11.0 1.0 ND1 B:HIS507 4.1 16.6 1.0 CG B:HIS507 4.1 18.3 1.0 CB B:ASP529 4.2 13.5 1.0 CZ B:PHE538 4.3 13.1 1.0 CE2 B:PHE538 4.3 9.8 1.0 O B:HOH2061 4.5 23.8 1.0 CB B:ALA504 4.5 12.3 1.0 C B:VAL505 4.5 16.3 1.0 CA B:ALA504 4.6 14.0 1.0 O B:HOH2067 4.6 21.6 1.0 CG2 B:VAL505 4.7 18.6 1.0 CA B:GLY531 4.7 16.9 1.0 C B:ALA504 4.8 14.3 1.0 CA B:VAL505 4.9 16.1 1.0 CD2 B:LEU513 5.0 15.6 1.0 N B:GLY531 5.0 17.0 1.0 CB B:GLU537 5.0 10.8 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