Sodium in PDB 5hap: Oxa-48 Beta-Lactamase - S70A Mutant

All present enzymatic activity of Oxa-48 Beta-Lactamase - S70A Mutant:
3.5.2.6;

The structure of Oxa-48 Beta-Lactamase - S70A Mutant, PDB code: 5hap was solved by V.Stojanoski, C.J.Adamski, L.Hu, S.C.Mehta, B.Sankaran, B.V.V.Prasad, T.G.Palzkill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.02 / 1.89
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.900, 121.900, 161.451, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 22.6

The structure of Oxa-48 Beta-Lactamase - S70A Mutant also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Sodium atom in the Oxa-48 Beta-Lactamase - S70A Mutant (pdb code 5hap). 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-48 Beta-Lactamase - S70A Mutant, PDB code: 5hap:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Oxa-48 Beta-Lactamase - S70A Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Oxa-48 Beta-Lactamase - S70A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Na305 b:41.5 occ:1.00 O A:ASN63 2.4 20.6 1.0 O A:HOH506 2.5 27.2 1.0 O A:HOH483 2.8 29.4 1.0 C A:ASN63 3.4 21.3 1.0 CA A:GLN64 3.7 19.3 1.0 N A:GLN64 4.0 18.8 1.0 N A:ALA65 4.0 16.6 1.0 C A:GLN64 4.3 21.6 1.0 CA A:ASN63 4.6 21.3 1.0 CB A:ALA65 4.7 18.9 1.0 CB A:ASN63 4.7 20.1 1.0 O A:HOH431 4.7 23.4 1.0 O A:HOH442 4.8 35.7 1.0 CG A:GLN64 4.9 29.5 1.0 CB A:GLN64 4.9 27.2 1.0 CA A:ALA65 5.0 18.5 1.0

Sodium binding site 2 out of 2 in the Oxa-48 Beta-Lactamase - S70A Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Oxa-48 Beta-Lactamase - S70A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Na301 b:41.7 occ:1.00 O B:HOH468 2.5 35.1 1.0 O B:HOH438 2.5 36.5 1.0 O B:ASN179 2.9 23.3 1.0 O B:HOH477 3.7 38.6 1.0 CB B:GLU185 3.7 20.5 1.0 CB B:ASN179 3.8 19.6 1.0 NE2 B:GLN188 3.9 17.8 1.0 CA B:GLU185 3.9 19.7 1.0 C B:ASN179 4.0 20.6 1.0 N B:GLU185 4.0 17.7 1.0 CA B:ASN179 4.5 20.5 1.0 CG B:GLU185 4.5 18.6 1.0 O B:HOH478 4.5 21.8 1.0 OE1 B:GLU185 4.5 27.3 1.0 O B:VAL183 4.5 20.3 1.0 C B:SER184 4.7 19.5 1.0 CG B:ASN179 4.9 27.1 1.0 CD B:GLN188 5.0 16.0 1.0

V.Stojanoski, C.J.Adamski, L.Hu, S.C.Mehta, B.Sankaran, P.Zwart, B.V.Prasad, T.Palzkill. Removal of the Side Chain at the Active-Site Serine By A Glycine Substitution Increases the Stability of A Wide Range of Serine Beta-Lactamases By Relieving Steric Strain. Biochemistry V. 55 2479 2016.
ISSN: ISSN 0006-2960
PubMed: 27073009
DOI: 10.1021/ACS.BIOCHEM.6B00056