Chlorine in PDB 5har: Oxa-163 Beta-Lactamase - S70G Mutant

All present enzymatic activity of Oxa-163 Beta-Lactamase - S70G Mutant:
3.5.2.6;

The structure of Oxa-163 Beta-Lactamase - S70G Mutant, PDB code: 5har 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)	62.38 / 1.74
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	44.340, 87.980, 124.770, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 22.1

The binding sites of Chlorine atom in the Oxa-163 Beta-Lactamase - S70G Mutant (pdb code 5har). 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-163 Beta-Lactamase - S70G Mutant, PDB code: 5har:

Chlorine binding site 1 out of 1 in the Oxa-163 Beta-Lactamase - S70G Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Oxa-163 Beta-Lactamase - S70G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:23.5 occ:0.42 O A:HOH605 2.5 32.5 1.0 NH2 A:ARG206 3.0 12.8 1.0 NH1 A:ARG206 3.1 12.1 1.0 CZ A:ARG206 3.5 11.9 1.0 CA A:GLN193 4.3 12.6 1.0 CD2 A:LEU196 4.3 10.6 1.0 CG A:GLN193 4.3 12.3 1.0 CB A:GLN193 4.6 12.5 1.0 NE A:ARG206 4.8 11.3 1.0 O A:GLN193 4.9 13.9 1.0 CB A:LEU196 4.9 10.7 1.0 O A:HOH484 5.0 30.4 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