Sodium in PDB 5mox: Oxa-10 Avibactam Complex with Bound CO2

All present enzymatic activity of Oxa-10 Avibactam Complex with Bound CO2:
3.5.2.6;

The structure of Oxa-10 Avibactam Complex with Bound CO2, PDB code: 5mox was solved by J.Brem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.76 / 1.41
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.751, 96.635, 126.363, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 19.1

The binding sites of Sodium atom in the Oxa-10 Avibactam Complex with Bound CO2 (pdb code 5mox). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Oxa-10 Avibactam Complex with Bound CO2, PDB code: 5mox:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Oxa-10 Avibactam Complex with Bound CO2


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 CO2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na302 b:23.5 occ:1.00 O A:HOH695 3.0 38.0 1.0 O A:HOH713 3.0 36.7 1.0 NE A:ARG250 3.1 11.7 1.0 NH1 A:ARG250 3.3 14.2 1.0 CZ A:ARG250 3.7 11.2 1.0 CD A:LYS251 3.8 28.7 1.0 CA A:PRO248 3.9 14.1 1.0 O A:LEU247 4.1 13.6 1.0 CG A:ARG250 4.1 11.8 1.0 CG A:LYS251 4.1 22.7 1.0 CD A:ARG250 4.2 11.4 1.0 N A:PRO248 4.5 13.6 1.0 C A:LEU247 4.5 13.1 1.0 CB A:LYS251 4.6 19.0 1.0 CB A:PRO248 4.7 16.1 1.0 O A:PRO248 4.7 15.0 1.0 C A:PRO248 4.7 14.1 1.0 O A:HOH504 4.7 22.4 1.0 CG A:LEU247 4.9 14.9 1.0 CG2 A:THR206 5.0 13.8 1.0 NH2 A:ARG250 5.0 11.3 1.0

Sodium binding site 2 out of 2 in the Oxa-10 Avibactam Complex with Bound CO2


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Oxa-10 Avibactam Complex with Bound CO2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Na302 b:25.7 occ:1.00 O B:HOH532 2.8 20.9 1.0 NZ B:LYS70 2.9 17.2 1.0 O B:HOH597 3.2 15.5 1.0 O B:HOH626 3.2 10.7 1.0 NE1 B:TRP154 3.3 17.9 1.0 CE B:LYS70 3.4 15.2 1.0 CG B:LYS70 3.5 12.0 1.0 O B:HOH633 3.8 21.6 1.0 CA B:SER67 4.0 11.1 1.0 CD B:LYS70 4.0 14.9 1.0 OG B:SER67 4.0 13.7 1.0 CE2 B:TRP154 4.1 15.3 1.0 CD1 B:TRP154 4.2 15.6 1.0 CZ2 B:TRP154 4.4 15.5 1.0 CB B:PHE120 4.4 12.2 1.0 CB B:SER67 4.5 12.7 1.0 O B:ALA66 4.6 11.8 1.0 N B:SER67 4.7 9.8 1.0 O B:SER67 4.8 10.2 1.0 CG2 B:VAL117 4.8 16.3 1.0 C B:SER67 4.8 10.3 1.0 CB B:LYS70 4.8 11.2 1.0 C B:ALA66 4.9 10.6 1.0 CA B:VAL117 4.9 16.2 1.0 CAN B:NXL301 4.9 14.3 1.0 N B:LYS70 5.0 9.1 1.0 CG B:PHE120 5.0 12.3 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