Zinc 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:

Sodium

(Na)

2 atoms

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

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo-Beta-Lactamase (C181S Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:18.8 occ:1.00 NE2 A:HIS99 2.2 16.6 1.0 NE2 A:HIS162 2.2 23.1 1.0 ND1 A:HIS101 2.3 6.4 1.0 O A:HOH250 2.5 19.0 1.0 CD2 A:HIS162 2.9 22.6 1.0 CG A:HIS101 3.1 12.8 1.0 CD2 A:HIS99 3.1 22.4 1.0 CB A:HIS101 3.1 13.8 1.0 CE1 A:HIS99 3.2 14.7 1.0 CE1 A:HIS162 3.3 27.5 1.0 CE1 A:HIS101 3.4 16.1 1.0 OD1 A:ASP103 3.6 30.1 1.0 CG A:HIS162 4.1 19.1 1.0 OD2 A:ASP103 4.1 21.4 1.0 ND1 A:HIS162 4.2 21.9 1.0 OG A:SER181 4.3 24.2 1.0 CG A:ASP103 4.3 24.3 1.0 CD2 A:HIS101 4.3 13.5 1.0 CG A:HIS99 4.3 19.6 1.0 ND1 A:HIS99 4.3 16.8 1.0 CB A:SER181 4.4 17.4 1.0 NE2 A:HIS101 4.4 11.3 1.0 CA A:HIS101 4.6 15.8 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo-Beta-Lactamase (C181S Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1 b:30.2 occ:1.00 NE2 B:HIS162 2.2 16.8 1.0 ND1 B:HIS101 2.3 5.4 1.0 NE2 B:HIS99 2.3 18.5 1.0 O B:HOH250 3.0 26.9 1.0 CG B:HIS101 3.1 6.0 1.0 CD2 B:HIS162 3.1 18.7 1.0 CE1 B:HIS162 3.2 21.6 1.0 CB B:HIS101 3.3 9.3 1.0 CE1 B:HIS99 3.3 13.9 1.0 CD2 B:HIS99 3.3 16.6 1.0 CE1 B:HIS101 3.4 5.0 1.0 OD1 B:ASP103 3.7 38.8 1.0 OG B:SER181 4.0 17.2 1.0 CB B:SER181 4.2 17.9 1.0 ND1 B:HIS162 4.3 19.4 1.0 CG B:HIS162 4.3 17.4 1.0 OD2 B:ASP103 4.3 30.4 1.0 CD2 B:HIS101 4.3 9.9 1.0 ND1 B:HIS99 4.4 11.2 1.0 CG B:HIS99 4.4 15.0 1.0 NE2 B:HIS101 4.4 9.5 1.0 CG B:ASP103 4.5 30.4 1.0 CA B:HIS101 4.7 15.4 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