Sodium in PDB 5fq9: Crystal Structure of the OXA10 with 1C

All present enzymatic activity of Crystal Structure of the OXA10 with 1C:
3.5.2.6;

The structure of Crystal Structure of the OXA10 with 1C, PDB code: 5fq9 was solved by J.Brem, M.A.Mcdonough, R.Cain, I.Clifton, C.W.G.Fishwick, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.42 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.898, 103.109, 125.529, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 18.1

The structure of Crystal Structure of the OXA10 with 1C also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Sodium atom in the Crystal Structure of the OXA10 with 1C (pdb code 5fq9). 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 the OXA10 with 1C, PDB code: 5fq9:

Sodium binding site 1 out of 1 in the Crystal Structure of the OXA10 with 1C


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 the OXA10 with 1C within 5.0Å range: probe atom residue distance (Å) B Occ B:Na500 b:32.3 occ:1.00 OE2 B:GLU171 3.0 28.4 1.0 N B:GLY20 3.2 27.1 1.0 CD B:GLU171 3.7 28.7 1.0 OE1 B:GLU171 3.8 31.8 1.0 CB B:CYS44 3.8 17.0 1.0 SG B:CYS51 3.9 21.9 1.0 CA B:GLY20 4.0 24.9 1.0 CA B:MET19 4.0 30.3 1.0 C B:MET19 4.1 28.9 1.0 CG B:MET19 4.1 37.9 1.0 SG B:CYS44 4.2 22.5 1.0 CA B:LYS49 4.3 25.2 1.0 C B:LYS49 4.3 26.2 1.0 N B:SER50 4.4 19.4 1.0 O B:HOH2002 4.4 50.9 1.0 O B:LYS45 4.7 20.0 1.0 CB B:MET19 4.7 33.9 1.0 CA B:CYS44 4.9 17.0 1.0 O B:LYS49 4.9 24.0 1.0

J.Brem, R.Cain, S.Cahill, M.A.Mcdonough, I.J.Clifton, J.C.Jimenez-Castellanos, M.B.Avison, J.Spencer, C.W.Fishwick, C.J.Schofield. Structural Basis of Metallo-Beta-Lactamase, Serine-Beta-Lactamase and Penicillin-Binding Protein Inhibition By Cyclic Boronates. Nat Commun V. 7 12406 2016.
ISSN: ESSN 2041-1723
PubMed: 27499424
DOI: 10.1038/NCOMMS12406