Chlorine in PDB 7r3r: Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme

All present enzymatic activity of Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme:
3.5.2.6;

The structure of Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme, PDB code: 7r3r was solved by C.L.Tooke, P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.94 / 1.17
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.553, 45.653, 117.876, 90, 90, 90
R / Rfree (%)	15.4 / 18.7

The binding sites of Chlorine atom in the Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme (pdb code 7r3r). 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 Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme, PDB code: 7r3r:

Chlorine binding site 1 out of 1 in the Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Ctx-M-15 G238C Mutant Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:15.2 occ:1.00 H A:LYS269 2.5 16.6 1.0 HB3 A:GLN267 2.8 16.5 1.0 HD2 A:PRO268 2.8 20.0 1.0 HB2 A:LYS269 2.8 21.5 1.0 N A:LYS269 3.3 13.8 1.0 HG3 A:LYS269 3.5 26.9 1.0 CB A:LYS269 3.6 17.9 1.0 CD A:PRO268 3.6 16.6 1.0 CB A:GLN267 3.7 13.8 1.0 N A:PRO268 3.8 14.6 1.0 HD2 A:LYS269 3.8 31.2 1.0 CA A:LYS269 3.9 14.1 1.0 CG A:LYS269 4.0 22.4 1.0 HB2 A:PRO268 4.0 20.4 1.0 HB2 A:GLN267 4.1 16.5 1.0 C A:GLN267 4.2 12.3 1.0 HG2 A:GLN267 4.3 17.3 1.0 HG2 A:PRO268 4.3 22.3 1.0 HD3 A:PRO268 4.3 20.0 1.0 HA A:GLN267 4.3 15.1 1.0 C A:PRO268 4.3 13.9 1.0 CA A:GLN267 4.4 12.6 1.0 CG A:PRO268 4.4 18.6 1.0 C A:LYS269 4.4 14.2 1.0 HB3 A:LYS269 4.4 21.5 1.0 CA A:PRO268 4.4 14.3 1.0 CD A:LYS269 4.4 26.0 1.0 CB A:PRO268 4.5 17.0 1.0 H A:ALA270 4.6 14.9 1.0 CG A:GLN267 4.6 14.4 1.0 N A:ALA270 4.7 12.4 1.0 HA A:LYS269 4.8 16.9 1.0 HG2 A:LYS269 4.9 26.9 1.0 O A:GLN267 4.9 13.7 1.0 HG3 A:GLN267 4.9 17.3 1.0 HE3 A:LYS269 4.9 37.8 1.0

P.Hinchliffe, C.L.Tooke, C.R.Bethel, B.Wang, C.Arthur, K.J.Heesom, S.Shapiro, D.M.Schlatzer, K.M.Papp-Wallace, R.A.Bonomo, J.Spencer. Penicillanic Acid Sulfones Inactivate the Extended-Spectrum Beta-Lactamase Ctx-M-15 Through Formation of A Serine-Lysine Cross-Link: An Alternative Mechanism of Beta-Lactamase Inhibition. Mbio V. 13 79321 2022.
ISSN: ESSN 2150-7511
PubMed: 35612361
DOI: 10.1128/MBIO.01793-21