Zinc in PDB 2nze: Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121.

All present enzymatic activity of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121.:
3.5.2.6;

The structure of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121., PDB code: 2nze was solved by F.J.Medrano Martin, A.J.Vila, J.M.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.62 / 1.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.665, 66.665, 175.947, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 21.7

The binding sites of Zinc atom in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121. (pdb code 2nze). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121., PDB code: 2nze:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:21.0 occ:1.00 O A:HOH812 1.8 19.9 1.0 ND1 A:HIS88 2.0 21.1 1.0 NE2 A:HIS149 2.0 15.7 1.0 NE2 A:HIS86 2.1 14.3 1.0 O A:HOH726 2.5 25.1 1.0 CE1 A:HIS86 3.0 16.3 1.0 CE1 A:HIS88 3.0 18.4 1.0 CD2 A:HIS149 3.0 13.2 1.0 CG A:HIS88 3.0 20.6 1.0 CE1 A:HIS149 3.1 16.0 1.0 CD2 A:HIS86 3.1 16.1 1.0 CB A:HIS88 3.4 22.2 1.0 OD1 A:ASP90 4.0 27.5 1.0 NE2 A:HIS88 4.1 19.7 1.0 ND1 A:HIS86 4.1 16.6 1.0 CD2 A:HIS88 4.1 21.6 1.0 CG A:HIS149 4.1 14.9 1.0 ND1 A:HIS149 4.1 14.7 1.0 OG A:SER168 4.2 18.0 1.0 CG A:HIS86 4.2 15.4 1.0 O A:HOH758 4.2 43.7 1.0 CG2 A:THR150 4.3 17.3 1.0 CB A:SER168 4.5 15.9 1.0 CD2 A:HIS91 4.6 23.4 1.0 O A:HOH765 4.7 28.4 1.0 OD2 A:ASP90 4.7 31.9 1.0 CG A:ASP90 4.8 28.1 1.0 CA A:HIS88 4.8 22.3 1.0 NE2 A:HIS91 4.9 25.3 1.0

Zinc binding site 2 out of 2 in the Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Beta-Lactamase II From Bacillus Cereus. R121H, C221S Double Mutant. Space Group P3121. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:23.9 occ:1.00 ND1 B:HIS88 1.9 23.9 1.0 NE2 B:HIS149 2.0 17.6 1.0 O B:HOH816 2.0 22.9 1.0 NE2 B:HIS86 2.1 17.9 1.0 O B:HOH785 2.5 25.6 1.0 CE1 B:HIS88 2.8 23.8 1.0 CG B:HIS88 2.9 26.1 1.0 CD2 B:HIS149 3.0 15.8 1.0 CE1 B:HIS149 3.0 18.1 1.0 CE1 B:HIS86 3.1 19.3 1.0 CD2 B:HIS86 3.1 17.6 1.0 CB B:HIS88 3.3 27.0 1.0 NE2 B:HIS88 3.9 25.7 1.0 OG B:SER168 4.0 18.0 1.0 CD2 B:HIS88 4.0 25.9 1.0 ND1 B:HIS149 4.1 16.2 1.0 CG B:HIS149 4.1 16.5 1.0 ND1 B:HIS86 4.2 18.3 1.0 O B:HOH749 4.2 39.5 1.0 CG B:HIS86 4.2 15.8 1.0 CB B:SER168 4.3 17.9 1.0 NE2 B:HIS91 4.4 28.8 1.0 CG2 B:THR150 4.4 16.2 1.0 OD1 B:ASP90 4.5 34.9 1.0 CD2 B:HIS91 4.5 27.7 1.0 CA B:HIS88 4.8 27.3 1.0 O B:HOH850 4.9 25.3 1.0

J.M.Gonzalez, F.J.Medrano Martin, A.L.Costello, D.L.Tierney, A.J.Vila. The ZN2 Position in Metallo-Beta-Lactamases Is Critical For Activity: A Study on Chimeric Metal Sites on A Conserved Protein Scaffold. J.Mol.Biol. V. 373 1141 2007.
ISSN: ISSN 0022-2836
PubMed: 17915249
DOI: 10.1016/J.JMB.2007.08.031