Zinc in PDB 2wrs: Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa

All present enzymatic activity of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa:
3.5.2.6;

The structure of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa, PDB code: 2wrs was solved by P.Lassaux, M.Hamel, M.Gulea, H.Delbruck, D.A.K.Traore, P.S.Mercuri, L.Horsfall, D.Dehareng, A.-C.Gaumont, J.-M.Frere, J.-L.Ferrer, K.Hoffmann, M.Galleni, C.Bebrone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.27 / 2.79
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	140.130, 45.670, 105.030, 90.00, 105.41, 90.00
R / Rfree (%)	19.861 / 25.318

The binding sites of Zinc atom in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa (pdb code 2wrs). 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 Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa, PDB code: 2wrs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa


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 Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1262 b:38.3 occ:1.00 ND1 A:HIS116 2.1 30.7 1.0 NE2 A:HIS179 2.1 24.9 1.0 OB2 A:FLC1263 2.2 58.4 1.0 NE2 A:HIS114 2.3 23.1 1.0 CG A:HIS116 2.9 28.9 1.0 CE1 A:HIS179 3.0 25.9 1.0 CE1 A:HIS116 3.1 31.6 1.0 CD2 A:HIS114 3.2 23.8 1.0 CB A:HIS116 3.2 25.6 1.0 CBC A:FLC1263 3.2 60.0 1.0 OHB A:FLC1263 3.3 62.1 1.0 CD2 A:HIS179 3.3 23.6 1.0 CE1 A:HIS114 3.3 23.8 1.0 CB A:FLC1263 3.9 61.9 1.0 OD1 A:ASP118 3.9 26.8 1.0 CD2 A:HIS116 4.1 29.7 1.0 SG A:CYS198 4.1 29.5 1.0 OB1 A:FLC1263 4.1 55.5 1.0 NE2 A:HIS116 4.1 31.4 1.0 ND1 A:HIS179 4.2 24.6 1.0 CAC A:FLC1263 4.3 63.5 1.0 CG A:HIS179 4.3 21.6 1.0 CB A:CYS198 4.4 27.7 1.0 ND1 A:HIS114 4.4 24.4 1.0 CG A:HIS114 4.4 20.8 1.0 OA2 A:FLC1263 4.4 63.2 1.0 OD2 A:ASP118 4.4 29.2 1.0 OA1 A:FLC1263 4.5 64.7 1.0 CG A:ASP118 4.6 27.9 1.0 CA A:HIS116 4.7 25.7 1.0 CA A:FLC1263 4.7 62.6 1.0 ND2 A:ASN210 5.0 52.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa


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 Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1262 b:58.5 occ:1.00 ND1 B:HIS116 1.9 49.0 1.0 OG2 B:FLC1263 2.1 70.9 1.0 NE2 B:HIS179 2.3 59.0 1.0 NE2 B:HIS114 2.7 51.1 1.0 CG B:HIS116 2.8 48.4 1.0 OB1 B:FLC1263 2.9 71.8 1.0 CE1 B:HIS116 3.0 49.0 1.0 CE1 B:HIS179 3.1 59.6 1.0 CB B:HIS116 3.1 46.9 1.0 CGC B:FLC1263 3.2 70.9 1.0 CD2 B:HIS179 3.4 60.0 1.0 CE1 B:HIS114 3.5 50.5 1.0 CD2 B:HIS114 3.7 49.5 1.0 CBC B:FLC1263 3.7 71.1 1.0 OD1 B:ASP118 3.9 46.9 1.0 SG B:CYS198 3.9 57.9 1.0 CD2 B:HIS116 4.0 49.0 1.0 NE2 B:HIS116 4.0 49.7 1.0 OG1 B:FLC1263 4.1 71.0 1.0 CB B:CYS198 4.1 57.5 1.0 CG B:FLC1263 4.1 70.8 1.0 OA1 B:FLC1263 4.2 69.5 1.0 ND1 B:HIS179 4.3 60.4 1.0 CB B:FLC1263 4.4 71.0 1.0 CAC B:FLC1263 4.4 69.6 1.0 CG B:HIS179 4.5 60.1 1.0 OB2 B:FLC1263 4.5 70.1 1.0 CA B:HIS116 4.6 47.0 1.0 ND1 B:HIS114 4.6 49.4 1.0 OD2 B:ASP118 4.7 46.3 1.0 CG B:ASP118 4.7 46.3 1.0 CA B:FLC1263 4.7 70.4 1.0 CG B:HIS114 4.7 47.6 1.0 OA2 B:FLC1263 4.8 69.4 1.0 N B:HIS116 4.9 46.6 1.0

P.Lassaux, M.Hamel, M.Gulea, H.Delbruck, P.S.Mercuri, L.Horsfall, D.Dehareng, M.Kupper, J.-M.Frere, K.Hoffmann, M.Galleni, C.Bebrone. Mercaptophosphonate Compounds As Broad-Spectrum Inhibitors of the Metallo-Beta-Lactamases. J.Med.Chem. V. 53 4862 2010.
ISSN: ISSN 0022-2623
PubMed: 20527888
DOI: 10.1021/JM100213C