Chlorine in PDB 6b1h: Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 4234 By Co- Crystallization

All present enzymatic activity of Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 4234 By Co- Crystallization:
3.5.2.6;

The structure of Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 4234 By Co- Crystallization, PDB code: 6b1h was solved by F.Van Den Akker, N.Q.Nhuyen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.36 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	34.487, 37.372, 81.831, 87.78, 89.96, 84.53
R / Rfree (%)	16.2 / 21

The binding sites of Chlorine atom in the Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 4234 By Co- Crystallization (pdb code 6b1h). 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 4234 By Co- Crystallization, PDB code: 6b1h:
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 4234 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 4234 By Co- Crystallization within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:16.1 occ:1.00 O A:HOH530 3.1 9.7 1.0 O B:HOH487 3.2 27.2 1.0 CB A:ASN100 3.4 15.8 1.0 NH1 B:ARG178 3.4 10.8 1.0 N A:ASN100 3.6 14.7 1.0 CA A:GLY98 3.7 8.1 1.0 CD B:ARG178 3.7 9.0 1.0 CG B:ARG164 3.8 6.8 1.0 CG A:ASN100 3.8 17.4 1.0 C A:GLY98 3.9 9.5 1.0 O B:HOH459 4.0 13.3 1.0 CD B:ARG164 4.0 7.1 1.0 CA A:ASN100 4.1 15.1 1.0 N A:LYS99 4.1 11.0 1.0 ND2 A:ASN100 4.2 17.4 1.0 N A:GLY98 4.3 7.5 1.0 O B:ASP163 4.4 6.7 1.0 OD1 A:ASN100 4.4 19.9 1.0 CB B:ASP163 4.4 7.3 1.0 O A:GLY98 4.4 8.7 1.0 CZ B:ARG178 4.4 9.9 1.0 NE B:ARG178 4.5 9.1 1.0 C A:LYS99 4.6 13.9 1.0 C B:ASP163 4.8 6.8 1.0 N A:ALA101 4.8 13.3 1.0 C A:ASN100 4.8 14.9 1.0 CA A:LYS99 4.9 13.4 1.0 CG B:ARG178 4.9 8.4 1.0 O3 B:SO4302 4.9 30.2 1.0 NE B:ARG164 4.9 7.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure Kpc-2 Beta-Lactamase Complexed with Wck 4234 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 4234 By Co- Crystallization within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl305 b:22.9 occ:1.00 OD1 B:ASN100 3.3 21.2 1.0 O B:HOH485 3.5 15.1 1.0 CB B:ASN100 3.5 16.9 1.0 N B:ASN100 3.7 13.5 1.0 CA B:GLY98 3.7 11.0 1.0 CG B:ASN100 3.8 18.4 1.0 C B:GLY98 3.9 12.0 1.0 CA B:ASN100 4.0 14.2 1.0 N B:GLY98 4.2 10.1 1.0 N B:LYS99 4.3 13.0 1.0 O B:GLY98 4.3 11.6 1.0 N B:ALA101 4.3 12.2 1.0 C B:ASN100 4.4 13.0 1.0 C B:LYS99 4.8 12.6 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