Chlorine in PDB 6yen: Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133)

All present enzymatic activity of Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133):
3.5.2.6;

The structure of Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133), PDB code: 6yen was solved by P.A.Lang, J.Brem, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	97.04 / 1.42
Space group	P 43 3 2
Cell size a, b, c (Å), α, β, γ (°)	137.229, 137.229, 137.229, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 16.9

The structure of Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133) also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133) (pdb code 6yen). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133), PDB code: 6yen:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133)


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 Ampc From E. Coli with Taniborbactam (Vnrx-5133) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl410 b:24.3 occ:0.33 ZN A:ZN408 2.2 19.2 0.3 NE2 A:HIS13 3.4 18.2 1.0 CD2 A:HIS13 3.5 19.4 1.0 CG A:ARG14 3.8 34.4 1.0 O A:HOH663 4.4 26.0 0.6 CD A:ARG14 4.6 37.9 1.0 CE1 A:HIS13 4.7 19.0 1.0 CG A:HIS13 4.9 18.7 1.0 CB A:ARG14 5.0 27.1 1.0 CA A:ARG14 5.0 21.4 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl411 b:38.2 occ:1.00 O A:HOH727 3.0 34.7 1.0 N A:GLY320 3.1 21.1 1.0 CG2 A:VAL211 3.8 29.9 1.0 CA A:VAL211 3.8 28.3 1.0 CA A:GLY320 3.9 21.4 1.0 C33 A:KJK401 4.0 45.3 1.0 CB A:THR319 4.0 20.5 1.0 C A:THR319 4.1 20.7 1.0 CB A:VAL211 4.2 29.1 1.0 CA A:THR319 4.2 19.3 1.0 N A:SER212 4.2 37.7 1.0 O A:HOH633 4.4 25.0 1.0 C A:VAL211 4.6 33.3 1.0 O A:HOH674 4.6 34.0 1.0 N A:VAL211 4.7 25.9 1.0 C23 A:KJK401 4.7 38.0 1.0 CG2 A:THR319 4.9 21.0 1.0 O A:HIS210 4.9 27.4 1.0 C24 A:KJK401 4.9 43.1 1.0 OG1 A:THR319 4.9 21.2 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Ampc From E. Coli with Taniborbactam (Vnrx-5133) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl412 b:38.1 occ:1.00 OE2 A:GLU171 2.8 34.2 0.5 NE2 A:GLN175 3.0 31.3 0.4 N A:ILE189 3.0 22.0 1.0 N A:ASN190 3.5 24.9 1.0 CD A:GLU171 3.7 33.9 0.5 CB A:ILE189 3.7 23.7 1.0 CA A:ILE189 3.8 21.6 1.0 NE2 A:GLN175 3.8 36.6 0.6 CG A:GLU171 3.8 31.5 0.5 CA A:TRP188 3.8 21.9 1.0 C A:TRP188 3.9 21.2 1.0 O A:ASN190 4.0 28.4 1.0 CD A:GLN175 4.0 29.6 0.4 C A:ILE189 4.2 23.3 1.0 CG A:GLN175 4.2 25.6 0.4 O A:HOH546 4.2 46.4 1.0 CE3 A:TRP188 4.2 29.4 1.0 CB A:TRP188 4.2 25.1 1.0 CG1 A:ILE189 4.5 26.2 1.0 CA A:ASN190 4.5 26.8 1.0 C A:ASN190 4.6 27.7 1.0 CB A:ASN190 4.8 30.6 1.0 CD1 A:ILE189 4.8 28.9 1.0 CE2 A:PHE179 4.9 22.1 1.0 CG2 A:ILE189 4.9 25.1 1.0 OE1 A:GLU171 4.9 35.3 0.5 O A:THR187 4.9 22.7 1.0 ND2 A:ASN190 5.0 33.4 1.0 CD2 A:TRP188 5.0 28.7 1.0

P.A.Lang, A.Parkova, T.M.Leissing, K.Calvopina, R.Cain, A.Krajnc, T.D.Panduwawala, J.Philippe, C.W.G.Fishwick, P.Trapencieris, M.G.P.Page, C.J.Schofield, J.Brem. Bicyclic Boronates As Potent Inhibitors of Ampc, the Class C Beta-Lactamase From Escherichia Coli Biomolecules 2020.
ISSN: ESSN 2218-273X
DOI: 10.3390/BIOM10060899