Chlorine in PDB 7l8o: Oxa-48 Bound By Compound 4.3

All present enzymatic activity of Oxa-48 Bound By Compound 4.3:
3.5.2.6;

The structure of Oxa-48 Bound By Compound 4.3, PDB code: 7l8o was solved by D.M.Taylor, L.Hu, B.V.V.Prasad, T.Palzkill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.60 / 2.70
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	122.039, 122.039, 160.787, 90, 90, 120
R / Rfree (%)	16.8 / 21.1

The structure of Oxa-48 Bound By Compound 4.3 also contains other interesting chemical elements:

Sodium

(Na)

4 atoms

The binding sites of Chlorine atom in the Oxa-48 Bound By Compound 4.3 (pdb code 7l8o). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Oxa-48 Bound By Compound 4.3, PDB code: 7l8o:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Oxa-48 Bound By Compound 4.3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Oxa-48 Bound By Compound 4.3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:93.4 occ:1.00 NH1 A:ARG186 3.0 30.2 1.0 NE A:ARG186 3.7 31.5 1.0 CB A:ASP88 3.8 38.5 1.0 CZ A:ARG186 3.8 34.9 1.0 OD2 A:ASP88 4.0 51.0 1.0 CG A:ASP88 4.4 43.5 1.0 O A:LYS87 4.7 42.3 1.0

Chlorine binding site 2 out of 5 in the Oxa-48 Bound By Compound 4.3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Oxa-48 Bound By Compound 4.3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:88.1 occ:1.00 OE1 A:GLU89 4.0 46.6 1.0 NE2 A:HIS90 4.4 54.0 1.0 CE1 A:HIS90 4.4 56.4 1.0 NE2 A:GLN193 4.6 27.4 1.0

Chlorine binding site 3 out of 5 in the Oxa-48 Bound By Compound 4.3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Oxa-48 Bound By Compound 4.3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl407 b:53.0 occ:1.00 O B:HOH510 2.8 31.4 1.0 O B:ALA207 2.9 26.1 1.0 O B:HOH517 2.9 20.8 1.0 CG B:MET115 3.8 32.4 1.0 CD B:LYS208 3.8 19.2 1.0 O B:MET195 3.9 28.6 1.0 C B:ALA207 3.9 26.3 1.0 CA B:LYS208 3.9 23.8 1.0 OG1 B:THR197 4.0 24.8 1.0 O B:ALA194 4.1 18.4 1.0 CA B:MET195 4.1 25.2 1.0 O B:MET115 4.3 34.6 1.0 C B:MET195 4.3 26.0 1.0 SD B:MET115 4.4 37.6 1.0 O B:HOH502 4.4 22.1 1.0 N B:LYS208 4.4 21.3 1.0 CA B:LYS116 4.4 36.3 1.0 CB B:LYS208 4.5 22.2 1.0 C B:MET115 4.5 35.8 1.0 N B:LYS116 4.6 36.2 1.0 CE B:LYS208 4.6 19.4 1.0 CG B:LYS208 4.7 23.1 1.0 NZ B:LYS208 4.8 21.7 1.0 O B:LEU196 4.8 31.6 1.0 CB B:MET115 4.9 30.4 1.0 N B:THR209 4.9 21.8 1.0 C B:ALA194 4.9 23.7 1.0 CB B:MET195 5.0 24.3 1.0

Chlorine binding site 4 out of 5 in the Oxa-48 Bound By Compound 4.3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Oxa-48 Bound By Compound 4.3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl403 b:34.0 occ:1.00 NH2 C:ARG206 3.2 21.6 1.0 NH1 C:ARG206 3.3 23.4 1.0 CZ C:ARG206 3.7 23.6 1.0 CD2 C:LEU196 4.3 24.2 1.0 CA C:GLN193 4.3 19.6 1.0 CG C:GLN193 4.4 24.0 1.0 CB C:GLN193 4.5 21.3 1.0 CB C:LEU196 4.9 28.1 1.0 O C:GLN193 4.9 23.0 1.0

Chlorine binding site 5 out of 5 in the Oxa-48 Bound By Compound 4.3


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Oxa-48 Bound By Compound 4.3 within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl504 b:52.8 occ:1.00 NH2 D:ARG206 3.3 22.4 1.0 NH1 D:ARG206 3.4 26.4 1.0 CZ D:ARG206 3.8 26.6 1.0 CD2 D:LEU196 4.2 22.6 1.0 CG D:GLN193 4.3 23.3 1.0 CA D:GLN193 4.3 21.0 1.0 CB D:GLN193 4.5 21.1 1.0 O D:GLN193 4.8 29.8 1.0 CB D:LEU196 4.9 27.0 1.0 CG D:LEU196 5.0 26.8 1.0

D.M.Taylor, L.Hu, B.V.V.Prasad, T.Palzkill. Unique Diacidic Fragments Inhibit the Oxa-48 Carbapenemase and Enhance the Killing of Escherichia Coli Producing Oxa-48 Acs Infect Dis. 2021.
ISSN: ESSN 2373-8227
DOI: 10.1021/ACSINFECDIS.1C00501