Chlorine in PDB 2iyy: Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4

All present enzymatic activity of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4:
2.7.1.71;

The structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4, PDB code: 2iyy was solved by M.D.Hartmann, G.P.Bourenkov, A.Oberschall, N.Strizhov, H.D.Bartunik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.16 / 1.62
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	59.349, 59.349, 102.867, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 23.3

The structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4 also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Chlorine atom in the Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4 (pdb code 2iyy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4, PDB code: 2iyy:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl214 b:35.6 occ:1.00 OE1 A:GLU61 2.7 18.9 1.0 OG A:SER85 2.8 20.9 1.0 O A:ARG58 2.8 20.6 1.0 CD A:GLU61 3.4 21.2 1.0 CG A:GLU61 3.4 22.8 1.0 CB A:SER85 3.5 22.3 1.0 CB A:GLU61 3.5 17.3 1.0 N A:GLU62 3.6 17.8 1.0 CA A:ARG58 3.6 18.1 1.0 C A:ARG58 3.6 18.8 1.0 CB A:ARG58 3.7 17.3 1.0 CD A:ARG58 3.8 22.9 1.0 O A:ALA82 3.9 17.0 1.0 CA A:GLU62 4.0 18.9 1.0 CB A:GLU62 4.0 26.0 1.0 CG2 A:VAL88 4.1 18.0 1.0 C A:GLU61 4.1 16.4 1.0 CA A:ALA82 4.1 18.9 1.0 CA A:GLU61 4.4 17.9 1.0 CG A:ARG58 4.4 21.6 1.0 O A:HOH2134 4.4 36.7 1.0 C A:ALA82 4.5 17.9 1.0 OE2 A:GLU61 4.5 18.9 1.0 O A:HOH2133 4.6 28.5 1.0 CB A:ALA82 4.7 21.3 1.0 CA A:SER85 4.8 19.8 1.0 O A:GLY81 4.8 20.1 1.0 O A:GLU61 4.8 19.9 1.0 N A:ARG59 4.9 24.2 1.0 N A:SER85 4.9 19.9 1.0 N A:ARG58 4.9 19.8 1.0 N A:GLU61 4.9 21.2 1.0 NH1 A:ARG58 5.0 21.2 1.0

Chlorine binding site 2 out of 2 in the Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Shikimate-3-Phosphate and SO4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl215 b:37.4 occ:0.50 O A:ARG20 2.0 22.9 0.5 O A:HOH2012 2.7 52.0 1.0 O A:HOH2049 2.9 55.8 1.0 C A:ARG20 3.0 15.8 0.5 O A:ARG20 3.1 19.5 0.5 CA A:ARG20 3.3 23.4 0.5 N A:LYS24 3.4 28.8 0.5 CB A:LYS24 3.4 19.7 0.5 CG A:ARG20 3.5 30.8 0.5 CG A:ARG20 3.7 37.9 0.5 CB A:ALA23 3.7 18.0 0.5 CA A:LYS24 3.8 26.1 0.5 CA A:ARG20 3.8 17.1 0.5 C A:ARG20 3.8 11.9 0.5 N A:LYS24 3.8 19.4 0.5 CB A:ARG20 3.9 28.4 0.5 CB A:ALA23 4.0 27.6 0.5 C A:ALA23 4.2 28.2 0.5 N A:ARG21 4.2 30.0 0.5 CB A:ARG20 4.3 19.9 0.5 CB A:LYS24 4.3 23.7 0.5 CA A:LYS24 4.4 14.6 0.5 CA A:ALA23 4.4 20.8 0.5 C A:ALA23 4.5 21.4 0.5 N A:ALA23 4.5 24.1 0.5 O A:HOH2053 4.5 39.3 1.0 CG A:LYS24 4.5 35.2 0.5 O A:GLY19 4.6 24.4 0.5 N A:ARG20 4.7 27.3 0.5 CA A:ALA23 4.7 17.0 0.5 CD A:LYS24 4.7 43.7 0.5 O A:HOH2014 4.7 47.1 1.0 CA A:ARG21 4.8 18.8 0.5 O A:ARG21 4.8 27.1 0.5 O A:GLY19 4.8 20.0 0.5 C A:ARG21 4.8 27.0 0.5 CD A:ARG20 4.9 53.4 0.5 O A:VAL28 5.0 31.2 0.5 O A:HOH2028 5.0 46.5 1.0 CD A:ARG20 5.0 26.5 0.5

M.D.Hartmann, G.P.Bourenkov, A.Oberschall, N.Strizhov, H.D.Bartunik. Mechanism of Phosphoryl Transfer Catalyzed By Shikimate Kinase From Mycobacterium Tuberculosis. J.Mol.Biol. V. 364 411 2006.
ISSN: ISSN 0022-2836
PubMed: 17020768
DOI: 10.1016/J.JMB.2006.09.001