Sodium in PDB 8btw: Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam

All present enzymatic activity of Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam:
3.5.2.6;

The structure of Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam, PDB code: 8btw was solved by A.Chikunova, S.Bruenle, M.Ubbink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.97 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.819, 54.452, 79.517, 90, 90, 90
R / Rfree (%)	16.1 / 20.2

The binding sites of Sodium atom in the Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam (pdb code 8btw). 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 Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam, PDB code: 8btw:

Sodium binding site 1 out of 1 in the Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of D179N Blac From Mycobacterium Tuberculosis in Complex with Vaborbactam within 5.0Å range: probe atom residue distance (Å) B Occ A:Na308 b:37.9 occ:1.00 O A:HOH535 3.2 29.3 1.0 O A:GLN110 3.2 20.0 1.0 N A:VAL113 3.6 21.1 1.0 CB A:VAL113 3.7 23.6 1.0 C A:GLN111 3.8 19.1 1.0 CG2 A:VAL113 3.9 22.7 1.0 CA A:GLN111 3.9 19.3 1.0 N A:HIS112 4.0 20.3 1.0 C A:GLN110 4.1 18.0 1.0 O A:GLN111 4.1 17.6 1.0 CA A:VAL113 4.2 23.0 1.0 N A:GLN111 4.4 18.2 1.0 N A:GLN114 4.5 26.4 1.0 C A:HIS112 4.6 21.5 1.0 CA A:HIS112 4.7 21.0 1.0 C A:VAL113 4.9 24.6 1.0 CG1 A:VAL113 4.9 25.4 1.0

I.Van Alen, A.Chikunova, D.B.Van Zanten, A.A.De Block, M.Timmer, S.Brunle, M.Ubbink. ASP179 in the Class A Beta-Lactamase From Mycobacterium Tuberculosis Is A Conserved Yet Not Essential Residue Due to Epistasis. Febs J. 2023.
ISSN: ISSN 1742-464X
PubMed: 37335937
DOI: 10.1111/FEBS.16892