Sodium in PDB 4tro: Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid

All present enzymatic activity of Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid:
1.3.1.9;

The structure of Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid, PDB code: 4tro was solved by A.Chollet, S.Julien, L.Mourey, L.Maveyraud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.40
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	97.434, 97.434, 139.752, 90.00, 90.00, 120.00
R / Rfree (%)	12.1 / 15.1

The binding sites of Sodium atom in the Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid (pdb code 4tro). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid, PDB code: 4tro:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid within 5.0Å range: probe atom residue distance (Å) B Occ A:Na309 b:31.9 occ:1.00 O A:HOH666 2.2 39.5 1.0 O A:HOH627 2.4 46.3 1.0 O A:ALA226 2.4 21.8 1.0 O A:ASP223 2.5 25.0 1.0 O A:HOH612 2.6 52.3 1.0 O A:GLN224 2.8 29.1 1.0 C A:GLN224 3.4 24.2 1.0 C A:ALA226 3.4 20.8 1.0 C A:ASP223 3.6 24.9 1.0 CA A:GLN224 3.8 24.5 1.0 N A:ALA226 3.8 20.3 1.0 CA A:ALA226 4.1 19.7 1.0 N A:GLN224 4.2 22.6 1.0 N A:ARG225 4.2 22.9 1.0 N A:GLY229 4.3 21.9 1.0 C A:ARG225 4.3 21.9 1.0 CA A:GLY229 4.3 23.0 1.0 N A:PRO227 4.4 19.6 1.0 O A:HOH464 4.5 61.5 1.0 O A:HOH644 4.5 58.5 1.0 CB A:ALA226 4.5 20.3 1.0 CA A:PRO227 4.6 21.6 1.0 C A:PRO227 4.7 23.2 1.0 O A:ARG225 4.7 23.1 1.0 CA A:ARG225 4.8 25.7 1.0 OD1 A:ASP223 4.8 28.1 1.0 CA A:ASP223 4.9 24.4 1.0 O A:PRO227 4.9 24.4 1.0

Sodium binding site 2 out of 2 in the Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis Inha, Inhibited with the Active Metabolite of Isoniazid within 5.0Å range: probe atom residue distance (Å) B Occ A:Na310 b:54.7 occ:1.00 OD1 A:ASP248 2.5 38.2 1.0 O A:HOH470 2.6 36.8 1.0 O A:GLY141 2.8 30.3 1.0 CG A:ASP248 3.4 45.5 1.0 O A:HOH558 3.6 41.6 1.0 C A:GLY141 3.7 25.8 1.0 CA A:ASP248 3.8 26.5 1.0 CA A:GLY141 3.9 27.1 1.0 NH2 A:ARG185 3.9 33.6 1.0 CB A:ASP248 3.9 35.1 1.0 NZ A:LYS8 4.1 37.2 1.0 O A:SER247 4.3 25.1 1.0 O A:HOH419 4.3 35.4 1.0 N A:ASP248 4.4 23.9 1.0 OD2 A:ASP248 4.5 94.1 1.0 C A:SER247 4.6 22.7 1.0 O A:HOH472 4.7 58.3 1.0 O A:HOH429 4.8 35.3 1.0 N A:GLY142 4.9 24.3 1.0 CZ A:ARG185 4.9 29.7 1.0 C A:ASP248 4.9 23.0 1.0 O A:HOH508 4.9 33.8 1.0

A.Chollet, L.Mourey, C.Lherbet, A.Delbot, S.Julien, M.Baltas, J.Bernadou, G.Pratviel, L.Maveyraud, V.Bernardes-Genisson. Crystal Structure of the Enoyl-Acp Reductase of Mycobacterium Tuberculosis (Inha) in the Apo-Form and in Complex with the Active Metabolite of Isoniazid Pre-Formed By A Biomimetic Approach. J.Struct.Biol. 2015.
ISSN: ESSN 1095-8657
PubMed: 25891098
DOI: 10.1016/J.JSB.2015.04.008