Chlorine in PDB 6b1w: Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization

All present enzymatic activity of Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization:
3.5.2.6;

The structure of Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization, PDB code: 6b1w was solved by F.Van Den Akker, N.Q.Nguyen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.35 / 1.73
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	34.528, 37.348, 82.068, 87.66, 89.71, 84.31
R / Rfree (%)	15.2 / 19.4

The binding sites of Chlorine atom in the Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization (pdb code 6b1w). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization, PDB code: 6b1w:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:22.7 occ:1.00 O A:HOH518 3.1 13.2 1.0 O B:HOH448 3.1 30.6 1.0 CB A:ASN100 3.4 21.5 1.0 NH1 B:ARG178 3.4 17.0 1.0 N A:ASN100 3.5 20.8 1.0 CA A:GLY98 3.6 12.7 1.0 CG A:ASN100 3.8 23.2 1.0 CD B:ARG178 3.8 16.2 1.0 C A:GLY98 3.8 14.5 1.0 CG B:ARG164 3.9 10.8 1.0 O B:HOH416 4.0 21.4 1.0 CA A:ASN100 4.0 21.6 1.0 N A:LYS99 4.1 17.4 1.0 ND2 A:ASN100 4.1 22.2 1.0 N A:GLY98 4.2 11.9 1.0 O B:ASP163 4.2 10.3 1.0 CD B:ARG164 4.2 11.9 1.0 OD1 A:ASN100 4.3 25.0 1.0 O A:GLY98 4.4 14.6 1.0 CB B:ASP163 4.4 11.9 1.0 CZ B:ARG178 4.4 16.9 1.0 NE B:ARG178 4.5 16.7 1.0 C A:LYS99 4.6 21.5 1.0 C B:ASP163 4.7 10.9 1.0 C A:ASN100 4.9 21.5 1.0 N A:ALA101 4.9 18.5 1.0 CA A:LYS99 4.9 20.9 1.0 O A:HOH493 4.9 35.5 1.0 CG B:ARG178 5.0 15.1 1.0 O3 B:SO4301 5.0 36.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 5107 By Co- Crystallization within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl305 b:23.8 occ:1.00 ND2 B:ASN100 3.4 17.2 1.0 CA B:GLY98 3.6 12.0 1.0 CB B:ASN100 3.6 15.9 1.0 N B:ASN100 3.6 14.5 1.0 C B:GLY98 3.8 12.7 1.0 O B:HOH509 3.8 20.8 1.0 CG B:ASN100 4.0 16.6 1.0 CA B:ASN100 4.1 14.8 1.0 N B:LYS99 4.1 13.3 1.0 N B:GLY98 4.2 11.5 1.0 O B:GLY98 4.2 11.3 1.0 N B:ALA101 4.4 13.2 1.0 C B:ASN100 4.6 13.4 1.0 C B:LYS99 4.7 14.2 1.0 CA B:LYS99 5.0 14.6 1.0

K.M.Papp-Wallace, N.Q.Nguyen, M.R.Jacobs, C.R.Bethel, M.D.Barnes, V.Kumar, S.Bajaksouzian, S.D.Rudin, P.N.Rather, S.Bhavsar, T.Ravikumar, P.K.Deshpande, V.Patil, R.Yeole, S.S.Bhagwat, M.V.Patel, F.Van Den Akker, R.A.Bonomo. Strategic Approaches to Overcome Resistance Against Gram-Negative Pathogens Using Beta-Lactamase Inhibitors and Beta-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes Wck 5153, Zidebactam (Wck 5107), and Wck 4234. J. Med. Chem. V. 61 4067 2018.
ISSN: ISSN 1520-4804
PubMed: 29627985
DOI: 10.1021/ACS.JMEDCHEM.8B00091