Sodium in PDB 7b3r: Oxa-10 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink

All present enzymatic activity of Oxa-10 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink:
3.5.2.6;

The structure of Oxa-10 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink, PDB code: 7b3r was solved by P.A.Lang, J.Brem, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.09 / 1.83
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.61, 95.457, 126.186, 90, 90, 90
R / Rfree (%)	17 / 19.1

The binding sites of Sodium atom in the Oxa-10 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink (pdb code 7b3r). 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 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink, PDB code: 7b3r:

Sodium binding site 1 out of 1 in the Oxa-10 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Oxa-10 Beta-Lactamase with S64DHA Modification and Lysinoalanine Crosslink within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:27.0 occ:1.00 O A:HOH569 2.8 29.9 1.0 O A:HOH595 3.0 40.4 1.0 N A:ALA98 3.1 20.9 1.0 CA A:ARG97 3.5 18.7 1.0 CG A:PRO118 3.6 24.9 1.0 CB A:ARG97 3.6 18.2 1.0 CZ3 A:TRP102 3.6 18.9 1.0 CE3 A:TRP102 3.7 18.1 1.0 C A:ARG97 3.8 20.3 1.0 CD A:PRO118 3.9 22.3 1.0 CB A:ALA98 4.0 28.1 1.0 CG A:ARG97 4.0 20.3 1.0 CA A:ALA98 4.1 23.6 1.0 CB A:PRO118 4.2 21.7 1.0 O A:PRO96 4.8 21.8 1.0 N A:ARG97 4.8 21.9 1.0 CD A:ARG97 4.9 22.0 1.0 CH2 A:TRP102 4.9 20.5 1.0 N A:PRO118 5.0 18.1 1.0

P.A.Lang, R.Raj, A.Tumber, C.T.Lohans, P.Rabe, C.V.Robinson, J.Brem, C.J.Schofield. Studies on Enmetazobactam Clarify Mechanisms of Widely Used Beta-Lactamase Inhibitors. Proc.Natl.Acad.Sci.Usa V. 119 10119 2022.
ISSN: ESSN 1091-6490
PubMed: 35486701
DOI: 10.1073/PNAS.2117310119