Sodium in PDB 5oe2: Crystal Structure of the Beta-Lactamase Oxa-245

All present enzymatic activity of Crystal Structure of the Beta-Lactamase Oxa-245:
3.5.2.6;

The structure of Crystal Structure of the Beta-Lactamase Oxa-245, PDB code: 5oe2 was solved by B.A.Lund, H.K.S.Leiros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.26 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.164, 108.720, 83.677, 90.00, 102.39, 90.00
R / Rfree (%)	19.1 / 22.6

The structure of Crystal Structure of the Beta-Lactamase Oxa-245 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of the Beta-Lactamase Oxa-245 (pdb code 5oe2). 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 Beta-Lactamase Oxa-245, PDB code: 5oe2:

Sodium binding site 1 out of 1 in the Crystal Structure of the Beta-Lactamase Oxa-245


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 Beta-Lactamase Oxa-245 within 5.0Å range: probe atom residue distance (Å) B Occ C:Na302 b:30.8 occ:1.00 H C:LEU111 2.2 35.0 1.0 HB2 C:LEU111 2.7 30.3 1.0 O C:ASP88 2.7 27.9 1.0 HE2 C:PHE93 2.9 48.5 1.0 N C:LEU111 2.9 29.1 1.0 O C:GLN91 3.0 33.7 1.0 HB2 C:ASN110 3.0 27.1 1.0 HB3 C:GLN91 3.0 39.3 1.0 HA C:GLU89 3.0 27.3 1.0 HG13 C:VAL86 3.2 43.5 1.0 H C:GLN91 3.2 35.7 1.0 CB C:LEU111 3.4 25.2 1.0 C C:GLU89 3.4 28.3 1.0 N C:GLN91 3.4 29.8 1.0 HA C:ASN110 3.4 29.7 1.0 HG11 C:VAL86 3.5 43.5 1.0 HB3 C:LEU111 3.5 30.3 1.0 O C:GLU89 3.6 29.0 1.0 CA C:GLU89 3.6 22.8 1.0 CA C:LEU111 3.7 24.9 1.0 CG1 C:VAL86 3.7 36.2 1.0 CE2 C:PHE93 3.8 40.4 1.0 CB C:ASN110 3.8 22.6 1.0 C C:ASP88 3.8 23.9 1.0 C C:GLN91 3.8 33.8 1.0 C C:ASN110 3.8 28.1 1.0 N C:HIS90 3.8 27.7 1.0 CB C:GLN91 3.8 32.7 1.0 CA C:ASN110 3.8 24.7 1.0 CA C:GLN91 3.9 32.9 1.0 HG12 C:VAL86 4.0 43.5 1.0 C C:HIS90 4.0 31.9 1.0 HA C:LEU111 4.1 29.9 1.0 H C:HIS90 4.1 33.2 1.0 N C:GLU89 4.2 25.2 1.0 HD2 C:PHE93 4.2 48.5 1.0 HB3 C:ASN110 4.2 27.1 1.0 HB2 C:GLN91 4.3 39.3 1.0 CD2 C:PHE93 4.4 40.4 1.0 CA C:HIS90 4.5 29.8 1.0 HD13 C:LEU111 4.5 26.7 1.0 H C:ASP88 4.6 30.1 1.0 HZ C:PHE93 4.7 51.6 1.0 CG C:LEU111 4.7 24.9 1.0 CZ C:PHE93 4.7 43.0 1.0 HA C:HIS90 4.7 35.8 1.0 H C:ILE112 4.7 30.1 1.0 O C:HIS90 4.8 30.9 1.0 HA C:GLN91 4.8 39.4 1.0 HD22 C:LEU111 4.8 27.5 1.0 HG2 C:GLN91 4.8 42.5 1.0 CG C:ASN110 4.9 25.6 1.0 O C:ASN110 4.9 30.1 1.0 CG C:GLN91 4.9 35.4 1.0 CB C:GLU89 5.0 22.8 1.0 HB2 C:GLU89 5.0 27.4 1.0

B.A.Lund, A.M.Thomassen, T.J.O.Carlsen, H.K.S.Leiros. Structure, Activity and Thermostability Investigations of Oxa-163, Oxa-181 and Oxa-245 Using Biochemical Analysis, Crystal Structures and Differential Scanning Calorimetry Analysis. Acta Crystallogr F Struct V. 73 579 2017BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 28994407
DOI: 10.1107/S2053230X17013838