Potassium in PDB 3veh: Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt

All present enzymatic activity of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt:
5.4.4.2;

The structure of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt, PDB code: 3veh was solved by E.M.Bulloch, G.Chi, A.Manos-Turvey, J.M.Johnston, E.N.Baker, R.J.Payne, J.S.Lott, Tb Structural Genomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.34 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.674, 115.955, 94.715, 90.00, 91.59, 90.00
R / Rfree (%)	17.5 / 23.6

The binding sites of Potassium atom in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt (pdb code 3veh). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt, PDB code: 3veh:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt within 5.0Å range: probe atom residue distance (Å) B Occ B:K504 b:50.8 occ:1.00 O A:HOH826 2.5 28.4 1.0 OE1 B:GLN240 2.7 28.3 1.0 O B:GLU43 2.7 18.6 1.0 O B:HOH703 2.8 26.6 1.0 OG1 B:THR38 3.3 17.8 1.0 O B:HOH815 3.5 33.4 1.0 NH1 A:ARG156 3.7 22.9 1.0 CB B:THR38 3.7 21.5 1.0 N B:GLU39 3.7 27.4 1.0 CD B:GLN240 3.9 24.1 1.0 C B:GLU43 3.9 20.8 1.0 CE2 B:TYR45 3.9 15.8 1.0 CD2 B:TYR45 4.0 16.5 1.0 CA B:GLU39 4.0 31.2 1.0 C B:THR38 4.0 26.1 1.0 NH2 A:ARG156 4.1 23.7 1.0 CZ A:ARG156 4.3 20.1 1.0 O B:THR38 4.4 23.4 1.0 CB B:GLU39 4.5 30.8 1.0 CA B:THR38 4.6 22.8 1.0 NE2 B:GLN240 4.7 23.4 1.0 O B:HOH603 4.7 21.0 1.0 N B:ASP44 4.7 20.6 1.0 O A:HOH660 4.7 31.2 1.0 CA B:ASP44 4.8 17.9 1.0 N B:GLU43 4.8 21.7 1.0 CG B:GLU39 4.9 35.5 1.0 CA B:GLU43 4.9 21.9 1.0 CG B:GLN240 4.9 18.5 1.0 CB B:GLN240 4.9 17.3 1.0 CG2 B:THR38 5.0 23.0 1.0

Potassium binding site 2 out of 2 in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor Methylamt within 5.0Å range: probe atom residue distance (Å) B Occ D:K502 b:56.7 occ:1.00 O D:HOH643 2.5 25.5 1.0 O D:HOH652 2.7 31.2 1.0 OG1 D:THR38 2.9 22.8 1.0 O D:HOH635 3.0 21.9 1.0 O D:ALA35 3.2 34.4 1.0 CB D:GLU39 3.6 27.3 1.0 N D:GLU39 3.6 23.3 1.0 O D:ALA34 3.6 32.6 1.0 CE2 D:TYR45 3.7 17.7 1.0 OE1 D:GLN240 3.9 28.9 1.0 CA D:GLU39 3.9 24.1 1.0 C D:ALA35 4.1 31.8 1.0 CB D:THR38 4.2 23.5 1.0 CA D:ALA35 4.2 29.0 1.0 O D:HOH651 4.3 28.1 1.0 C D:THR38 4.4 24.9 1.0 OE1 D:GLU39 4.4 49.7 1.0 CD2 D:TYR45 4.4 17.9 1.0 C D:ALA34 4.6 31.1 1.0 CZ D:TYR45 4.6 22.4 1.0 OH D:TYR45 4.6 19.8 1.0 CG D:GLU39 4.6 35.7 1.0 CA D:THR38 4.8 21.9 1.0 NH1 D:ARG245 4.9 24.4 1.0 N D:ALA35 4.9 30.8 1.0 CD D:GLN240 4.9 22.9 1.0

G.Chi, A.Manos-Turvey, P.D.O'connor, J.M.Johnston, G.L.Evans, E.N.Baker, R.J.Payne, J.S.Lott, E.M.Bulloch. Implications of Binding Mode and Active Site Flexibility For Inhibitor Potency Against the Salicylate Synthase From Mycobacterium Tuberculosis. Biochemistry V. 51 4868 2012.
ISSN: ISSN 0006-2960
PubMed: 22607697
DOI: 10.1021/BI3002067