Chlorine in PDB 6b2q: Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis

All present enzymatic activity of Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis:
2.7.11.1;

The structure of Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis, PDB code: 6b2q was solved by H.J.Zuccola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	113.72 / 2.88
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	79.065, 227.432, 158.606, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 26.3

The binding sites of Chlorine atom in the Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis (pdb code 6b2q). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis, PDB code: 6b2q:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:82.4 occ:1.00 CL22 A:CJJ301 0.0 82.4 1.0 C9 A:CJJ301 1.7 73.3 1.0 C10 A:CJJ301 2.7 67.2 1.0 C8 A:CJJ301 2.7 70.9 1.0 N12 A:CJJ301 3.0 62.2 1.0 O A:GLY100 3.1 59.7 1.0 O A:VAL98 3.2 52.9 1.0 N A:GLY100 3.6 54.2 1.0 C A:GLY100 3.9 58.2 1.0 N11 A:CJJ301 3.9 67.5 1.0 N7 A:CJJ301 4.0 70.0 1.0 CA A:GLY100 4.2 53.5 1.0 C A:VAL98 4.3 54.4 1.0 C13 A:CJJ301 4.4 58.9 1.0 C6 A:CJJ301 4.4 69.8 1.0 CG2 A:ILE19 4.5 66.6 1.0 C A:ASN99 4.5 58.8 1.0 CA A:ASN99 4.5 55.0 1.0 CD2 A:LEU148 4.8 62.8 1.0 N A:ASN99 4.9 53.1 1.0 CD1 A:ILE19 5.0 73.9 1.0

Chlorine binding site 2 out of 4 in the Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl300 b:82.3 occ:1.00 CL22 B:CJJ300 0.0 82.3 1.0 C9 B:CJJ300 1.7 77.3 1.0 C10 B:CJJ300 2.7 72.0 1.0 C8 B:CJJ300 2.7 78.2 1.0 N12 B:CJJ300 3.0 66.7 1.0 O B:VAL98 3.2 68.6 1.0 O B:GLY100 3.2 70.1 1.0 N B:GLY100 3.6 68.4 1.0 C B:GLY100 3.8 69.5 1.0 N11 B:CJJ300 3.9 74.4 1.0 N7 B:CJJ300 4.0 78.2 1.0 CA B:GLY100 4.2 67.0 1.0 C B:VAL98 4.3 69.4 1.0 C13 B:CJJ300 4.4 63.0 1.0 C6 B:CJJ300 4.4 79.2 1.0 C B:ASN99 4.6 74.1 1.0 CA B:ASN99 4.6 70.8 1.0 CG2 B:ILE19 4.7 90.0 1.0 N B:GLU101 4.8 64.7 1.0 N B:ASN99 4.9 68.7 1.0

Chlorine binding site 3 out of 4 in the Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl300 b:0.2 occ:1.00 CL22 C:CJJ300 0.0 0.2 1.0 C9 C:CJJ300 1.7 0.7 1.0 C8 C:CJJ300 2.7 0.2 1.0 C10 C:CJJ300 2.7 0.6 1.0 N12 C:CJJ300 3.0 0.2 1.0 O C:VAL98 3.2 0.8 1.0 O C:GLY100 3.3 0.1 1.0 N C:GLY100 3.7 0.5 1.0 N11 C:CJJ300 4.0 0.5 1.0 N7 C:CJJ300 4.0 0.5 1.0 C C:GLY100 4.2 0.2 1.0 CA C:ASN99 4.3 0.0 1.0 C C:VAL98 4.3 0.7 1.0 C13 C:CJJ300 4.4 0.9 1.0 C6 C:CJJ300 4.4 0.0 1.0 CG2 C:ILE19 4.5 0.9 1.0 C C:ASN99 4.5 0.2 1.0 CA C:GLY100 4.5 0.8 1.0 N C:ASN99 4.8 0.8 1.0 N18 C:CJJ300 4.9 0.7 1.0

Chlorine binding site 4 out of 4 in the Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Dual Inhibition of the Essential Protein Kinases A and B in Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl300 b:98.2 occ:1.00 CL22 D:CJJ300 0.0 98.2 1.0 C9 D:CJJ300 1.7 93.0 1.0 C8 D:CJJ300 2.7 93.4 1.0 C10 D:CJJ300 2.8 87.7 1.0 O D:GLY100 3.0 77.0 1.0 N12 D:CJJ300 3.1 82.3 1.0 O D:VAL98 3.1 66.3 1.0 N D:GLY100 3.7 73.1 1.0 N11 D:CJJ300 4.0 88.1 1.0 N7 D:CJJ300 4.0 92.2 1.0 C D:GLY100 4.0 77.3 1.0 CG2 D:ILE19 4.1 80.8 1.0 C D:VAL98 4.3 67.3 1.0 CA D:GLY100 4.4 72.9 1.0 C6 D:CJJ300 4.4 91.2 1.0 C13 D:CJJ300 4.5 76.1 1.0 CA D:ASN99 4.5 72.2 1.0 C D:ASN99 4.6 77.2 1.0 N D:ASN99 4.9 69.0 1.0

T.Wang, G.Bemis, B.Hanzelka, H.Zuccola, M.Wynn, C.S.Moody, J.Green, C.Locher, A.Liu, H.Gao, Y.Xu, S.Wang, J.Wang, Y.L.Bennani, J.A.Thomson, U.Muh. Mtb Pkna/Pknb Dual Inhibition Provides Selectivity Advantages For Inhibitor Design to Minimize Host Kinase Interactions. Acs Med Chem Lett V. 8 1224 2017.
ISSN: ISSN 1948-5875
PubMed: 29259738
DOI: 10.1021/ACSMEDCHEMLETT.7B00239