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

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

The structure of Crystal Structure of the Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa, PDB code: 2whg was solved by P.Lassaux, D.A.K.Traore, M.Galleni, J.L.Ferrer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.30 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	141.390, 46.220, 105.990, 90.00, 105.24, 90.00
R / Rfree (%)	20 / 25.4

The binding sites of Zinc atom in the Crystal Structure of the Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa (pdb code 2whg). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa, PDB code: 2whg:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of the Di-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 Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1262 b:20.4 occ:1.00 OD2 A:ASP118 2.1 15.9 1.0 OA2 A:FLC1264 2.1 17.1 1.0 NE2 A:HIS240 2.1 17.7 1.0 OB2 A:FLC1264 2.4 19.1 1.0 SG A:CYS198 2.4 15.5 1.0 OHB A:FLC1264 2.4 17.3 1.0 CBC A:FLC1264 3.0 17.4 1.0 CD2 A:HIS240 3.0 16.0 1.0 CB A:FLC1264 3.1 17.8 1.0 CG A:ASP118 3.1 14.3 1.0 CAC A:FLC1264 3.1 20.6 1.0 CE1 A:HIS240 3.2 15.3 1.0 CA A:FLC1264 3.6 18.5 1.0 OD1 A:ASP118 3.6 14.4 1.0 CB A:CYS198 3.6 12.8 1.0 ZN A:ZN1263 3.8 17.2 1.0 NH2 A:ARG119 4.0 15.2 1.0 OB1 A:FLC1264 4.2 15.1 1.0 OA1 A:FLC1264 4.2 23.4 1.0 CG A:HIS240 4.2 15.4 1.0 ND1 A:HIS240 4.3 14.4 1.0 OG1 A:FLC1264 4.3 18.5 1.0 O A:HOH2230 4.3 21.0 1.0 CB A:ASP118 4.4 13.7 1.0 CG A:FLC1264 4.5 18.1 1.0 NE A:ARG119 4.5 12.0 1.0 NE2 A:HIS179 4.6 11.9 1.0 CE1 A:HIS179 4.6 12.9 1.0 CZ A:ARG119 4.7 14.0 1.0 CE1 A:HIS114 4.7 9.4 1.0 NE2 A:HIS114 4.8 10.9 1.0 CA A:CYS198 4.8 14.5 1.0 CGC A:FLC1264 4.9 19.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the Di-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 Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1263 b:17.2 occ:1.00 OB2 A:FLC1264 1.9 19.1 1.0 ND1 A:HIS116 2.0 16.9 1.0 NE2 A:HIS179 2.1 11.9 1.0 NE2 A:HIS114 2.1 10.9 1.0 CBC A:FLC1264 2.7 17.4 1.0 OB1 A:FLC1264 2.9 15.1 1.0 CD2 A:HIS179 3.0 12.6 1.0 CE1 A:HIS114 3.0 9.4 1.0 CE1 A:HIS116 3.0 17.2 1.0 CE1 A:HIS179 3.0 12.9 1.0 CG A:HIS116 3.1 13.8 1.0 CD2 A:HIS114 3.1 10.9 1.0 CB A:HIS116 3.4 12.5 1.0 ZN A:ZN1262 3.8 20.4 1.0 ND1 A:HIS114 4.1 10.6 1.0 NE2 A:HIS116 4.1 17.5 1.0 OD1 A:ASP118 4.1 14.4 1.0 SG A:CYS198 4.1 15.5 1.0 CB A:FLC1264 4.1 17.8 1.0 ND1 A:HIS179 4.1 14.9 1.0 OA2 A:FLC1264 4.1 17.1 1.0 CG A:HIS179 4.1 13.7 1.0 CD2 A:HIS116 4.2 14.0 1.0 CB A:CYS198 4.2 12.8 1.0 CG A:HIS114 4.2 11.3 1.0 OHB A:FLC1264 4.6 17.3 1.0 OG1 A:FLC1264 4.6 18.5 1.0 OD2 A:ASP118 4.7 15.9 1.0 CG A:ASP118 4.8 14.3 1.0 CGC A:FLC1264 4.8 19.3 1.0 CA A:HIS116 4.8 13.1 1.0 CAC A:FLC1264 4.9 20.6 1.0 CG A:FLC1264 4.9 18.1 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the Di-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 3 of Crystal Structure of the Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1262 b:28.7 occ:1.00 OB2 B:FLC1264 1.9 24.6 1.0 ND1 B:HIS116 2.1 27.4 1.0 NE2 B:HIS179 2.1 29.5 1.0 NE2 B:HIS114 2.3 23.4 1.0 CBC B:FLC1264 2.7 26.5 1.0 OB1 B:FLC1264 2.8 25.8 1.0 CE1 B:HIS116 3.0 27.1 1.0 CD2 B:HIS179 3.1 29.1 1.0 CG B:HIS116 3.1 26.9 1.0 CE1 B:HIS179 3.1 28.8 1.0 CE1 B:HIS114 3.2 24.0 1.0 CD2 B:HIS114 3.2 23.0 1.0 CB B:HIS116 3.4 26.7 1.0 ZN B:ZN1263 3.8 27.5 1.0 OD1 B:ASP118 4.0 22.3 1.0 CB B:CYS198 4.1 26.4 1.0 SG B:CYS198 4.1 27.8 1.0 NE2 B:HIS116 4.1 27.7 1.0 CB B:FLC1264 4.1 26.4 1.0 ND1 B:HIS179 4.2 29.6 1.0 CG B:HIS179 4.2 30.3 1.0 CD2 B:HIS116 4.2 27.1 1.0 OA2 B:FLC1264 4.2 29.6 1.0 ND1 B:HIS114 4.3 23.7 1.0 CG B:HIS114 4.3 24.4 1.0 OHB B:FLC1264 4.5 24.6 1.0 OG1 B:FLC1264 4.6 28.3 1.0 OD2 B:ASP118 4.7 23.9 1.0 CG B:ASP118 4.8 23.4 1.0 CGC B:FLC1264 4.8 27.4 1.0 CA B:HIS116 4.8 26.4 1.0 CAC B:FLC1264 4.9 29.1 1.0 CG B:FLC1264 5.0 26.6 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the Di-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 4 of Crystal Structure of the Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1263 b:27.5 occ:1.00 NE2 B:HIS240 2.1 21.7 1.0 OA2 B:FLC1264 2.1 29.6 1.0 OD2 B:ASP118 2.1 23.9 1.0 OB2 B:FLC1264 2.3 24.6 1.0 OHB B:FLC1264 2.3 24.6 1.0 SG B:CYS198 2.4 27.8 1.0 CBC B:FLC1264 2.9 26.5 1.0 CB B:FLC1264 3.0 26.4 1.0 CE1 B:HIS240 3.1 20.8 1.0 CD2 B:HIS240 3.1 22.2 1.0 CAC B:FLC1264 3.1 29.1 1.0 CG B:ASP118 3.2 23.4 1.0 CA B:FLC1264 3.6 27.2 1.0 OD1 B:ASP118 3.6 22.3 1.0 CB B:CYS198 3.7 26.4 1.0 ZN B:ZN1262 3.8 28.7 1.0 NH2 B:ARG119 3.9 27.0 1.0 OB1 B:FLC1264 4.1 25.8 1.0 ND1 B:HIS240 4.2 21.1 1.0 CG B:HIS240 4.2 22.6 1.0 OG1 B:FLC1264 4.2 28.3 1.0 OA1 B:FLC1264 4.2 30.8 1.0 CG B:FLC1264 4.4 26.6 1.0 CB B:ASP118 4.4 23.4 1.0 O B:HOH2123 4.4 23.6 1.0 NE B:ARG119 4.6 24.2 1.0 NE2 B:HIS179 4.6 29.5 1.0 CE1 B:HIS179 4.7 28.8 1.0 CZ B:ARG119 4.7 25.8 1.0 CGC B:FLC1264 4.7 27.4 1.0 CE1 B:HIS114 4.8 24.0 1.0 NE2 B:HIS114 4.9 23.4 1.0 CA B:CYS198 4.9 26.5 1.0

P.Lassaux, D.A.K.Traore, E.Loisel, A.Favier, J.D.Docquier, J.S.Sohier, C.Laurent, C.Bebrone, J.M.Frere, J.L.Ferrer, M.Galleni. Biochemical and Structural Characterization of the Subclass B1 Metallo-{Beta}-Lactamase Vim-4. Antimicrob.Agents Chemother. V. 55 1248 2011.
ISSN: ISSN 0066-4804
PubMed: 21149620
DOI: 10.1128/AAC.01486-09