Sodium in PDB 5mnu: Oxa-10 Avibactam Complex with Bound Bromide

All present enzymatic activity of Oxa-10 Avibactam Complex with Bound Bromide:
3.5.2.6;

The structure of Oxa-10 Avibactam Complex with Bound Bromide, PDB code: 5mnu was solved by J.Brem, M.Mcdonough, I.Clifton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.66 / 1.56
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.771, 101.421, 127.221, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 20.8

The structure of Oxa-10 Avibactam Complex with Bound Bromide also contains other interesting chemical elements:

Bromine

(Br)

6 atoms

The binding sites of Sodium atom in the Oxa-10 Avibactam Complex with Bound Bromide (pdb code 5mnu). 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 Oxa-10 Avibactam Complex with Bound Bromide, PDB code: 5mnu:

Sodium binding site 1 out of 1 in the Oxa-10 Avibactam Complex with Bound Bromide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Oxa-10 Avibactam Complex with Bound Bromide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na310 b:24.5 occ:1.00 O A:HOH651 2.4 40.3 1.0 O A:HOH673 2.9 47.6 1.0 O A:HOH581 3.1 31.0 1.0 N A:LEU64 3.1 12.8 1.0 CA A:TYR63 3.6 12.5 1.0 CG A:LEU64 3.8 16.1 1.0 C A:TYR63 3.8 12.9 1.0 CB A:TYR63 3.8 13.4 1.0 CB A:LEU64 3.9 14.0 1.0 CD1 A:TYR63 4.0 15.2 1.0 NE A:ARG160 4.0 17.0 1.0 CA A:LEU64 4.0 12.4 1.0 CD A:ARG160 4.1 17.0 1.0 CD1 A:LEU64 4.1 15.3 1.0 O A:HOH680 4.2 30.5 1.0 CG A:TYR63 4.4 13.5 1.0 CZ A:ARG160 4.5 16.3 1.0 CG1 A:VAL219 4.5 14.4 1.0 O A:HOH407 4.7 19.1 0.5 O A:HOH681 4.8 48.8 1.0 O A:GLU62 4.9 15.9 1.0 N A:TYR63 4.9 12.5 1.0 CB A:VAL219 4.9 12.9 1.0 O A:HOH676 5.0 44.3 1.0 NH1 A:ARG160 5.0 18.3 1.0

C.T.Lohans, D.Y.Wang, C.Jorgensen, S.T.Cahill, I.J.Clifton, M.A.Mcdonough, H.P.Oswin, J.Spencer, C.Domene, T.D.W.Claridge, J.Brem, C.J.Schofield. (13)C-Carbamylation As A Mechanistic Probe For the Inhibition of Class D Beta-Lactamases By Avibactam and Halide Ions. Org. Biomol. Chem. V. 15 6024 2017.
ISSN: ESSN 1477-0539
PubMed: 28678295
DOI: 10.1039/C7OB01514C