Chlorine 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:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Oxa-48 Beta-Lactamase - S70A Mutant (pdb code 5hap). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Oxa-48 Beta-Lactamase - S70A Mutant, PDB code: 5hap:

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


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Oxa-48 Beta-Lactamase - S70A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:22.5 occ:1.00 O A:HOH553 3.0 25.6 1.0 NH2 A:ARG206 3.0 17.7 1.0 NH1 A:ARG206 3.0 15.1 1.0 NH2 B:ARG206 3.0 14.1 1.0 NH1 B:ARG206 3.1 13.6 1.0 CZ A:ARG206 3.4 17.0 1.0 CZ B:ARG206 3.5 16.6 1.0 CD2 B:LEU196 4.2 15.4 1.0 CG B:GLN193 4.2 17.9 1.0 CD2 A:LEU196 4.3 16.4 1.0 CA B:GLN193 4.3 16.5 1.0 CA A:GLN193 4.4 13.1 1.0 CG A:GLN193 4.4 14.9 1.0 CB B:GLN193 4.7 15.7 1.0 CB A:GLN193 4.7 16.5 1.0 NE A:ARG206 4.7 15.9 1.0 CB B:LEU196 4.8 13.3 1.0 CB A:LEU196 4.8 12.5 1.0 O B:GLN193 4.8 14.2 1.0 NE B:ARG206 4.8 14.2 1.0 O A:GLN193 4.9 15.9 1.0 CG A:LEU196 4.9 18.1 1.0 CG B:LEU196 4.9 14.7 1.0 CD1 A:LEU196 4.9 15.9 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