Mercury in PDB 3znb: Metallo-Beta-Lactamase (Zn, Hg-Bound Form)

All present enzymatic activity of Metallo-Beta-Lactamase (Zn, Hg-Bound Form):
3.5.2.6;

The structure of Metallo-Beta-Lactamase (Zn, Hg-Bound Form), PDB code: 3znb was solved by N.O.Concha, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	78.200, 78.200, 140.600, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 26.8

The structure of Metallo-Beta-Lactamase (Zn, Hg-Bound Form) also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Sodium	(Na)	2 atoms

The binding sites of Mercury atom in the Metallo-Beta-Lactamase (Zn, Hg-Bound Form) (pdb code 3znb). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Metallo-Beta-Lactamase (Zn, Hg-Bound Form), PDB code: 3znb:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Metallo-Beta-Lactamase (Zn, Hg-Bound Form)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Metallo-Beta-Lactamase (Zn, Hg-Bound Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg2 b:32.5 occ:1.00 SG A:CYS181 2.3 18.0 1.0 SG A:CYS104 2.3 15.1 1.0 OD2 A:ASP69 2.9 16.4 1.0 O A:HOH262 3.1 15.5 1.0 CE1 A:HIS99 3.5 13.6 1.0 O A:HOH258 3.5 4.1 1.0 O A:ASP103 3.7 12.4 1.0 CB A:CYS104 3.7 13.2 1.0 OD2 A:ASP103 3.8 23.6 1.0 CB A:CYS181 3.8 12.2 1.0 CG A:ASP103 3.9 16.2 1.0 OD1 A:ASP103 3.9 19.1 1.0 ND1 A:HIS99 4.0 7.9 1.0 CA A:CYS104 4.0 8.5 1.0 C A:ASP103 4.0 9.8 1.0 CB A:ASN98 4.1 2.0 1.0 CG A:ASP69 4.1 16.8 1.0 N A:CYS104 4.1 12.1 1.0 NE2 A:HIS99 4.2 17.7 1.0 OD1 A:ASN98 4.3 2.0 1.0 CG A:ASN98 4.6 2.0 1.0 OD1 A:ASP69 4.6 17.4 1.0 ZN A:ZN1 4.8 14.2 1.0 CB A:ASP103 4.8 9.7 1.0 N A:CYS181 4.8 13.7 1.0 NA A:NA3 4.9 14.2 1.0 CG A:HIS99 4.9 11.3 1.0 CA A:ASP103 5.0 10.3 1.0 CA A:CYS181 5.0 11.1 1.0

Mercury binding site 2 out of 2 in the Metallo-Beta-Lactamase (Zn, Hg-Bound Form)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Metallo-Beta-Lactamase (Zn, Hg-Bound Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg2 b:35.4 occ:1.00 SG B:CYS104 2.2 12.1 1.0 SG B:CYS181 2.5 5.2 1.0 OD2 B:ASP69 2.7 20.5 1.0 O B:HOH259 3.0 16.2 1.0 CB B:CYS104 3.5 12.4 1.0 O B:ASP103 3.6 14.2 1.0 CE1 B:HIS99 3.6 10.3 1.0 CA B:CYS104 3.8 10.7 1.0 CG B:ASP69 3.8 18.2 1.0 CB B:ASN98 3.9 2.0 1.0 C B:ASP103 3.9 10.9 1.0 N B:CYS104 3.9 11.2 1.0 ND1 B:HIS99 4.0 7.8 1.0 CB B:CYS181 4.0 8.8 1.0 CG B:ASP103 4.1 16.1 1.0 OD2 B:ASP103 4.1 20.0 1.0 OD1 B:ASP103 4.1 21.5 1.0 OD1 B:ASP69 4.2 25.6 1.0 OD1 B:ASN98 4.3 2.0 1.0 NA B:NA3 4.3 23.5 1.0 NE2 B:HIS99 4.4 15.9 1.0 CG B:ASN98 4.4 2.1 1.0 CB B:ASP103 4.8 11.5 1.0 N B:CYS181 4.9 14.1 1.0 CA B:ASP103 4.9 13.4 1.0 ZN B:ZN1 4.9 15.0 1.0 CG B:HIS99 4.9 11.1 1.0

N.O.Concha, B.A.Rasmussen, K.Bush, O.Herzberg. Crystal Structures of the Cadmium- and Mercury-Substituted Metallo-Beta-Lactamase From Bacteroides Fragilis. Protein Sci. V. 6 2671 1997.
ISSN: ISSN 0961-8368
PubMed: 9416622