Zinc in PDB 4nq4: Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7

All present enzymatic activity of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7:
3.5.2.6;

The structure of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7, PDB code: 4nq4 was solved by J.M.Gonzalez, M.M.Gonzalez, A.J.Vila, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.60 / 1.67
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.115, 60.810, 69.251, 90.00, 93.00, 90.00
R / Rfree (%)	24.3 / 30

The structure of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Zinc atom in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 (pdb code 4nq4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7, PDB code: 4nq4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:17.0 occ:1.00 ND1 A:HIS88 2.0 17.0 1.0 NE2 A:HIS149 2.0 12.8 1.0 NE2 A:HIS86 2.1 14.8 1.0 O A:HOH406 2.3 15.8 1.0 CE1 A:HIS88 2.9 18.6 1.0 CG A:HIS88 3.0 17.6 1.0 CE1 A:HIS149 3.0 15.0 1.0 CE1 A:HIS86 3.0 13.5 1.0 CD2 A:HIS149 3.1 11.8 1.0 CD2 A:HIS86 3.1 14.3 1.0 CB A:HIS88 3.3 16.9 1.0 O A:HOH532 3.7 24.3 1.0 ZN A:ZN302 3.7 22.2 1.0 OD1 A:ASP90 3.9 19.0 1.0 NE2 A:HIS88 4.0 17.5 1.0 CB A:CYS168 4.0 17.6 1.0 CD2 A:HIS88 4.1 18.2 1.0 ND1 A:HIS149 4.1 14.0 1.0 ND1 A:HIS86 4.1 14.5 1.0 CG A:HIS149 4.2 12.5 1.0 CG A:HIS86 4.2 14.2 1.0 CG2 A:THR150 4.3 15.4 1.0 SG A:CYS168 4.4 19.3 1.0 CA A:HIS88 4.8 17.1 1.0 CG A:ASP90 4.8 17.0 1.0 OD2 A:ASP90 4.8 21.1 1.0

Zinc binding site 2 out of 2 in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:22.2 occ:1.00 NE2 A:HIS210 2.1 20.7 1.0 OD2 A:ASP90 2.2 21.1 1.0 O A:HOH406 2.2 15.8 1.0 SG A:CYS168 2.3 19.3 1.0 CE1 A:HIS210 2.9 23.4 1.0 CG A:ASP90 3.0 17.0 1.0 CD2 A:HIS210 3.2 23.0 1.0 OD1 A:ASP90 3.3 19.0 1.0 CB A:CYS168 3.3 17.6 1.0 ZN A:ZN301 3.7 17.0 1.0 NE A:ARG91 4.0 21.6 1.0 NH1 A:ARG91 4.0 25.6 1.0 ND1 A:HIS210 4.0 23.6 1.0 CG A:HIS210 4.2 21.8 1.0 CB A:ASP90 4.3 19.8 1.0 CE1 A:HIS86 4.3 13.5 1.0 CZ A:ARG91 4.3 21.8 1.0 NE2 A:HIS86 4.4 14.8 1.0 NE2 A:HIS149 4.5 12.8 1.0 CA A:CYS168 4.6 15.1 1.0 O A:HOH532 4.7 24.3 1.0 O A:HOH533 4.8 29.9 1.0 CE1 A:HIS149 4.9 15.0 1.0 O A:GLY209 4.9 19.0 1.0 CD A:ARG91 4.9 18.5 1.0 O A:HOH404 5.0 22.6 1.0

M.M.Gonzalez, J.M.Gonzalez, A.J.Vila. Inhibition of Metallo-Lactamases with Bicyclic Compounds To Be Published.