Zinc in PDB 5ew0: Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319:
3.5.2.6;

The structure of Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319, PDB code: 5ew0 was solved by P.Hinchliffe, C.L.Tooke, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.42 / 1.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.770, 86.700, 72.230, 90.00, 90.09, 90.00
R / Rfree (%)	16 / 18.9

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319 (pdb code 5ew0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319, PDB code: 5ew0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:8.9 occ:1.00 OD2 A:ASP111 1.9 10.7 1.0 O10 A:3C7302 2.0 14.2 1.0 NE2 A:HIS247 2.0 6.6 1.0 SG A:CYS205 2.3 9.7 1.0 CE1 A:HIS247 2.9 7.0 1.0 CG A:ASP111 3.0 7.6 1.0 C09 A:3C7302 3.0 15.2 1.0 CD2 A:HIS247 3.1 7.4 1.0 CB A:CYS205 3.3 8.0 1.0 OD1 A:ASP111 3.3 7.9 1.0 C12 A:3C7302 3.3 18.1 1.0 C08 A:3C7302 3.3 14.3 1.0 NH2 A:ARG112 3.7 6.0 1.0 O11 A:3C7302 4.1 15.7 1.0 ND1 A:HIS247 4.1 7.0 1.0 CA A:CYS205 4.2 7.6 1.0 CG A:HIS247 4.2 7.4 1.0 CZ A:ARG112 4.3 5.4 1.0 CB A:ASP111 4.3 5.8 1.0 NE A:ARG112 4.3 4.8 1.0 CE1 A:HIS186 4.4 7.5 1.0 O A:HOH575 4.6 19.2 1.0 NE2 A:HIS186 4.6 6.8 1.0 N07 A:3C7302 4.8 14.1 1.0 N A:CYS205 5.0 6.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Metallo-Beta-Lactamase Sfh-I in Complex with the Bisthiazolidine Inhibitor L-CS319 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:10.7 occ:1.00 O10 B:3C7302 1.8 12.8 1.0 OD2 B:ASP111 1.9 12.3 1.0 NE2 B:HIS247 2.1 8.0 1.0 SG B:CYS205 2.3 9.8 1.0 C09 B:3C7302 2.9 11.8 1.0 CE1 B:HIS247 3.0 7.5 1.0 O B:HOH406 3.0 21.3 1.0 CG B:ASP111 3.0 8.8 1.0 CD2 B:HIS247 3.1 8.4 1.0 CB B:CYS205 3.3 9.8 1.0 OD1 B:ASP111 3.3 12.6 1.0 C12 B:3C7302 3.4 13.1 1.0 C08 B:3C7302 3.5 12.9 1.0 NH2 B:ARG112 3.8 6.2 1.0 O11 B:3C7302 4.0 10.4 1.0 ND1 B:HIS247 4.1 7.7 1.0 CG B:HIS247 4.2 8.1 1.0 CA B:CYS205 4.3 8.9 1.0 CB B:ASP111 4.3 7.8 1.0 CZ B:ARG112 4.3 7.8 1.0 NE B:ARG112 4.4 8.2 1.0 CE1 B:HIS186 4.4 7.4 1.0 NE2 B:HIS186 4.6 8.3 1.0 N07 B:3C7302 4.9 12.0 1.0 O B:HOH570 4.9 23.5 1.0 N B:CYS205 4.9 7.2 1.0

P.Hinchliffe, M.M.Gonzalez, M.F.Mojica, J.M.Gonzalez, V.Castillo, C.Saiz, M.Kosmopoulou, C.L.Tooke, L.I.Llarrull, G.Mahler, R.A.Bonomo, A.J.Vila, J.Spencer. Cross-Class Metallo-Beta-Lactamase Inhibition By Bisthiazolidines Reveals Multiple Binding Modes. Proc.Natl.Acad.Sci.Usa V. 113 E3745 2016.
ISSN: ESSN 1091-6490
PubMed: 27303030
DOI: 10.1073/PNAS.1601368113