Chlorine in PDB 7r3q: Crystal Structure of Ctx-M-15 G238C/A240 Insert Mutant Apoenzyme

All present enzymatic activity of Crystal Structure of Ctx-M-15 G238C/A240 Insert Mutant Apoenzyme:
3.5.2.6;

The structure of Crystal Structure of Ctx-M-15 G238C/A240 Insert Mutant Apoenzyme, PDB code: 7r3q 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)	58.95 / 1.46
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.475, 45.583, 117.9, 90, 90, 90
R / Rfree (%)	15.7 / 21.2

The binding sites of Chlorine atom in the Crystal Structure of Ctx-M-15 G238C/A240 Insert Mutant Apoenzyme (pdb code 7r3q). 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/A240 Insert Mutant Apoenzyme, PDB code: 7r3q:

Chlorine binding site 1 out of 1 in the Crystal Structure of Ctx-M-15 G238C/A240 Insert 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/A240 Insert Mutant Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:16.5 occ:1.00 H A:ALA227 2.4 17.4 1.0 HA A:PRO226 3.0 17.6 1.0 O A:HOH651 3.1 18.5 1.0 N A:ALA227 3.2 14.5 1.0 HB3 A:PRO226 3.4 17.8 1.0 HB3 A:ALA227 3.6 21.0 1.0 HB2 A:ALA227 3.7 21.0 1.0 CA A:PRO226 3.7 14.7 1.0 CB A:ALA227 4.0 17.5 1.0 C A:PRO226 4.0 13.5 1.0 CB A:PRO226 4.0 14.8 1.0 CA A:ALA227 4.2 16.2 1.0 H A:SER228 4.5 21.5 1.0 HB2 A:PRO226 4.6 17.8 1.0 HG3 A:PRO226 4.9 17.5 1.0 HA A:ALA227 4.9 19.4 1.0 HB1 A:ALA227 4.9 21.0 1.0 O A:HOH731 5.0 28.3 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