Magnesium in PDB 3rv6: Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group

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

The structure of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group, PDB code: 3rv6 was solved by G.Chi, E.M.M.Bulloch, A.Manos-Turvey, R.J.Payne, J.S.Lott, Tb Structuralgenomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.72 / 2.04
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.748, 91.530, 96.466, 90.00, 104.83, 90.00
R / Rfree (%)	17.1 / 20.5

The binding sites of Magnesium atom in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group (pdb code 3rv6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group, PDB code: 3rv6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:27.4 occ:1.00 O A:HOH561 1.9 21.8 1.0 O A:HOH560 2.0 26.6 1.0 O A:HOH556 2.1 42.5 1.0 O A:HOH559 2.1 28.1 1.0 O A:HOH554 2.2 30.2 1.0 O A:HOH555 2.3 43.3 1.0 O A:HOH586 3.7 27.4 1.0 OE1 A:GLU297 3.8 45.5 1.0 O A:GLY421 3.9 22.7 1.0 OE2 A:GLU297 4.2 24.5 1.0 O A:HOH719 4.3 24.1 1.0 OE2 A:GLU434 4.4 49.8 1.0 CD A:GLU297 4.4 38.7 1.0 OA' A:VAE451 4.5 24.2 1.0 OE1 A:GLU431 4.5 30.6 1.0 OB' A:VAE451 4.5 23.9 1.0 NZ A:LYS293 4.5 51.0 1.0 CD A:LYS293 4.5 51.0 1.0 N A:GLY421 4.5 16.9 1.0 CE A:LYS293 4.6 54.1 1.0 C' A:VAE451 4.8 24.2 1.0 C A:GLY421 4.8 22.6 1.0 CA A:GLY421 4.8 16.9 1.0 OE2 A:GLU294 4.9 48.7 1.0 CD A:GLU434 4.9 56.0 1.0 OE2 A:GLU431 5.0 43.6 1.0

Magnesium binding site 2 out of 2 in the Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of A M. Tuberculosis Salicylate Synthase, Mbti, in Complex with An Inhibitor with Phenyl R-Group within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg452 b:54.0 occ:1.00 O B:HOH562 2.1 32.8 1.0 O B:HOH575 2.1 26.3 1.0 O B:HOH676 2.5 53.8 1.0 OE2 B:GLU434 3.2 63.2 1.0 O B:HOH646 3.5 45.0 1.0 O B:HOH669 3.5 41.0 1.0 CD B:GLU434 3.6 65.9 1.0 CG B:GLU434 4.0 38.7 1.0 OE1 B:GLU297 4.1 68.2 1.0 OE1 B:GLU431 4.1 25.3 1.0 OE1 B:GLU434 4.3 75.3 1.0 O B:HOH656 4.5 50.2 1.0 O B:HOH732 4.5 52.1 1.0 OB' B:RVA451 4.7 40.4 1.0 O B:GLY421 4.7 25.0 1.0 OA' B:RVA451 4.8 36.5 1.0 CB B:GLU434 4.9 25.4 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