Sodium in PDB 6jcl: Crystal Structure of Cofactor-Bound RV0187 From Mtb

The structure of Crystal Structure of Cofactor-Bound RV0187 From Mtb, PDB code: 6jcl was solved by J.Kim, S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.23 / 1.64
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	75.300, 75.920, 329.839, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 20.7

The structure of Crystal Structure of Cofactor-Bound RV0187 From Mtb also contains other interesting chemical elements:

Strontium

(Sr)

10 atoms

The binding sites of Sodium atom in the Crystal Structure of Cofactor-Bound RV0187 From Mtb (pdb code 6jcl). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Cofactor-Bound RV0187 From Mtb, PDB code: 6jcl:

Sodium binding site 1 out of 1 in the Crystal Structure of Cofactor-Bound RV0187 From Mtb


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Cofactor-Bound RV0187 From Mtb within 5.0Å range: probe atom residue distance (Å) B Occ B:Na305 b:33.6 occ:1.00 O B:HOH401 2.5 35.9 1.0 O B:LEU198 2.7 26.4 1.0 O B:MET192 2.7 23.3 1.0 O B:GLY193 2.8 24.2 1.0 O B:HIS195 2.9 25.6 1.0 O B:HOH499 3.2 24.6 1.0 C B:GLY193 3.4 22.0 1.0 C B:LEU198 3.7 26.6 1.0 CA B:GLY193 3.7 19.6 1.0 C B:MET192 3.8 26.1 1.0 C B:HIS195 3.9 22.6 1.0 N B:HIS195 3.9 22.9 1.0 N B:GLU194 4.2 21.1 1.0 N B:GLY193 4.3 18.9 1.0 CB B:LEU198 4.3 22.6 1.0 C B:GLU194 4.4 25.0 1.0 CA B:HIS195 4.4 25.6 1.0 O B:HOH472 4.4 35.9 1.0 CA B:LEU198 4.5 20.4 1.0 N B:ASP199 4.5 19.9 1.0 CA B:ASP199 4.5 21.4 1.0 N B:LEU198 4.7 21.5 1.0 CA B:GLU194 4.7 24.4 1.0 CB B:HIS195 4.8 27.7 1.0 N B:ALA200 4.9 18.1 1.0 N B:PRO196 5.0 27.2 1.0

S.Lee, J.Kang, J.Kim. Structural and Biochemical Characterization of RV0187, An O-Methyltransferase From Mycobacterium Tuberculosis. Sci Rep V. 9 8059 2019.
ISSN: ESSN 2045-2322
PubMed: 31147608
DOI: 10.1038/S41598-019-44592-7