Sodium in PDB 4znb: Metallo-Beta-Lactamase (C181S Mutant)

All present enzymatic activity of Metallo-Beta-Lactamase (C181S Mutant):
3.5.2.6;

The structure of Metallo-Beta-Lactamase (C181S Mutant), PDB code: 4znb was solved by Z.Li, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.65
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	78.000, 78.000, 139.800, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 25

The structure of Metallo-Beta-Lactamase (C181S Mutant) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Sodium atom in the Metallo-Beta-Lactamase (C181S Mutant) (pdb code 4znb). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Metallo-Beta-Lactamase (C181S Mutant), PDB code: 4znb:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Metallo-Beta-Lactamase (C181S Mutant)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Metallo-Beta-Lactamase (C181S Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na3 b:14.2 occ:1.00 O A:ASP103 2.3 28.6 1.0 O A:ASN55 2.3 18.5 1.0 OD2 A:ASP69 2.6 9.6 1.0 O A:HOH256 2.6 24.4 1.0 CB A:ASP69 3.0 12.4 1.0 CG A:ASP69 3.2 11.4 1.0 C A:ASN55 3.4 15.6 1.0 C A:ASP103 3.5 22.8 1.0 O A:THR70 3.8 5.5 1.0 OH A:TYR40 4.0 28.5 1.0 N A:ASN55 4.2 15.4 1.0 N A:GLY56 4.3 13.2 1.0 CA A:ASP69 4.3 12.0 1.0 CA A:GLY56 4.3 14.2 1.0 OD1 A:ASP69 4.4 9.8 1.0 CA A:ASN55 4.4 16.9 1.0 N A:CYS104 4.4 17.5 1.0 CB A:ASP103 4.4 20.3 1.0 CA A:CYS104 4.5 11.0 1.0 CA A:ASP103 4.5 20.3 1.0 CB A:SER54 4.5 15.8 1.0 C A:ASP69 4.5 11.9 1.0 N A:THR70 4.5 10.0 1.0 C A:THR70 4.7 9.6 1.0 C A:SER54 4.7 20.9 1.0 CZ A:PHE178 4.7 6.9 1.0 OD2 A:ASP103 4.8 21.4 1.0 O A:GLY222 4.9 14.3 1.0 SG A:CYS104 4.9 16.2 1.0 CZ A:TYR40 4.9 12.3 1.0 CG A:ASP103 4.9 24.3 1.0

Sodium binding site 2 out of 2 in the Metallo-Beta-Lactamase (C181S Mutant)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Metallo-Beta-Lactamase (C181S Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Na3 b:18.4 occ:1.00 O B:ASN55 2.3 26.7 1.0 O B:ASP103 2.4 23.4 1.0 O B:HOH253 2.4 21.1 1.0 OD2 B:ASP69 2.6 27.7 1.0 C B:ASN55 3.3 22.2 1.0 CG B:ASP69 3.4 19.2 1.0 CB B:ASP69 3.5 14.6 1.0 C B:ASP103 3.5 21.3 1.0 N B:ASN55 3.8 18.3 1.0 CB B:SER54 4.0 31.6 1.0 CA B:ASN55 4.1 20.6 1.0 CB B:ASP103 4.1 25.3 1.0 C B:SER54 4.3 16.4 1.0 O B:THR70 4.3 17.9 1.0 OD2 B:ASP103 4.3 30.4 1.0 N B:GLY56 4.3 21.6 1.0 CA B:ASP103 4.4 22.0 1.0 O B:GLY222 4.4 22.3 1.0 N B:CYS104 4.5 18.2 1.0 CG B:ASP103 4.6 30.4 1.0 CA B:GLY56 4.6 20.7 1.0 OG B:SER54 4.6 46.1 1.0 OD1 B:ASP69 4.6 19.9 1.0 OH B:TYR40 4.7 23.0 1.0 CA B:SER54 4.7 22.7 1.0 CA B:CYS104 4.7 13.6 1.0 CZ B:PHE178 4.8 9.3 1.0 CA B:ASP69 4.8 10.9 1.0 O B:SER54 4.9 14.0 1.0

Z.Li, B.A.Rasmussen, O.Herzberg. Structural Consequences of the Active Site Substitution CYS181 --> Ser in Metallo-Beta-Lactamase From Bacteroides Fragilis. Protein Sci. V. 8 249 1999.
ISSN: ISSN 0961-8368
PubMed: 10210203