Zinc in PDB 4tze: Structure of Metallo-Beta-Lactamase

The structure of Structure of Metallo-Beta-Lactamase, PDB code: 4tze was solved by J.A.Ferguson, A.Makena, J.Brem, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.07 / 1.57
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.773, 59.216, 62.968, 90.00, 92.19, 90.00
R / Rfree (%)	19.5 / 23.4

The binding sites of Zinc atom in the Structure of Metallo-Beta-Lactamase (pdb code 4tze). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of Metallo-Beta-Lactamase, PDB code: 4tze:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Metallo-Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:18.1 occ:1.00 ND1 A:HIS122 2.0 13.3 1.0 NE2 A:HIS189 2.0 17.4 1.0 NE2 A:HIS120 2.0 12.4 1.0 O A:HOH426 2.1 20.4 1.0 CE1 A:HIS122 2.9 19.3 1.0 CD2 A:HIS189 2.9 17.9 1.0 CD2 A:HIS120 3.0 12.9 1.0 CE1 A:HIS120 3.0 21.4 1.0 CG A:HIS122 3.0 15.9 1.0 CE1 A:HIS189 3.0 19.6 1.0 CB A:HIS122 3.4 11.0 1.0 ZN A:ZN302 3.5 22.6 0.8 SG A:CYS208 3.7 21.3 1.0 CB A:CYS208 3.9 26.7 1.0 O A:HOH444 4.0 24.9 1.0 OD1 A:ASP124 4.0 21.5 1.0 NE2 A:HIS122 4.1 21.3 1.0 ND1 A:HIS120 4.1 19.3 1.0 CD2 A:HIS122 4.1 21.0 1.0 CG A:HIS189 4.1 22.3 1.0 CG A:HIS120 4.1 12.3 1.0 ND1 A:HIS189 4.1 22.1 1.0 OD2 A:ASP124 4.4 25.0 1.0 CG2 A:THR190 4.5 25.6 1.0 CG A:ASP124 4.6 17.1 1.0 CA A:HIS122 4.8 12.6 1.0

Zinc binding site 2 out of 4 in the Structure of Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Metallo-Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:22.6 occ:0.85 O A:HOH426 2.1 20.4 1.0 OD2 A:ASP124 2.1 25.0 1.0 NE2 A:HIS250 2.1 23.1 1.0 O A:HOH444 2.1 24.9 1.0 SG A:CYS208 2.4 21.3 1.0 CD2 A:HIS250 3.1 23.9 1.0 CE1 A:HIS250 3.1 21.8 1.0 CG A:ASP124 3.2 17.1 1.0 ZN A:ZN301 3.5 18.1 1.0 CB A:CYS208 3.6 26.7 1.0 OD1 A:ASP124 3.6 21.5 1.0 O A:HOH514 3.9 50.1 1.0 NE2 A:HIS189 4.1 17.4 1.0 ND1 A:HIS250 4.2 21.9 1.0 O A:HOH490 4.2 38.0 1.0 CG A:HIS250 4.2 21.0 1.0 CE1 A:HIS189 4.3 19.6 1.0 CB A:ASP124 4.5 11.7 1.0 NE2 A:HIS120 4.6 12.4 1.0 CB A:SER249 4.6 24.6 1.0 CA A:CYS208 4.7 22.7 1.0 CE1 A:HIS120 4.8 21.4 1.0 ND1 A:HIS122 5.0 13.3 1.0

Zinc binding site 3 out of 4 in the Structure of Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Metallo-Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:17.7 occ:0.98 NE2 B:HIS189 2.0 19.2 1.0 ND1 B:HIS122 2.0 17.4 1.0 O B:HOH434 2.1 20.5 1.0 NE2 B:HIS120 2.1 17.3 1.0 CD2 B:HIS189 2.9 20.9 1.0 CD2 B:HIS120 3.0 16.3 1.0 CG B:HIS122 3.0 13.1 1.0 CE1 B:HIS122 3.0 18.4 1.0 CE1 B:HIS189 3.0 19.8 1.0 CE1 B:HIS120 3.1 15.3 1.0 CB B:HIS122 3.3 15.4 1.0 ZN B:ZN302 3.6 24.2 0.9 SG B:CYS208 3.8 26.1 1.0 CB B:CYS208 3.9 23.9 1.0 OD1 B:ASP124 4.0 21.2 1.0 O B:HOH428 4.0 24.6 1.0 NE2 B:HIS122 4.1 17.9 1.0 CG B:HIS189 4.1 22.1 1.0 ND1 B:HIS189 4.1 19.7 1.0 CD2 B:HIS122 4.1 17.9 1.0 CG B:HIS120 4.1 16.9 1.0 ND1 B:HIS120 4.1 19.8 1.0 OD2 B:ASP124 4.5 20.6 1.0 CG2 B:THR190 4.5 21.0 1.0 O B:HOH515 4.6 48.1 1.0 CG B:ASP124 4.7 15.3 1.0 CA B:HIS122 4.8 14.5 1.0

Zinc binding site 4 out of 4 in the Structure of Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Metallo-Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:24.2 occ:0.88 NE2 B:HIS250 2.0 27.4 1.0 O B:HOH434 2.1 20.5 1.0 OD2 B:ASP124 2.1 20.6 1.0 O B:HOH428 2.1 24.6 1.0 SG B:CYS208 2.4 26.1 1.0 CE1 B:HIS250 3.0 27.7 1.0 CD2 B:HIS250 3.1 28.2 1.0 CG B:ASP124 3.2 15.3 1.0 O B:HOH517 3.4 50.2 1.0 CB B:CYS208 3.5 23.9 1.0 OD1 B:ASP124 3.6 21.2 1.0 ZN B:ZN301 3.6 17.7 1.0 ND1 B:HIS250 4.1 27.8 1.0 CG B:HIS250 4.2 30.2 1.0 NE2 B:HIS189 4.2 19.2 1.0 O B:HOH504 4.3 36.0 1.0 CE1 B:HIS189 4.4 19.8 1.0 CB B:ASP124 4.4 10.6 1.0 CB B:SER249 4.5 27.8 1.0 NE2 B:HIS120 4.6 17.3 1.0 CA B:CYS208 4.7 24.4 1.0 CE1 B:HIS120 4.8 15.3 1.0 OG B:SER249 4.9 27.5 1.0

J.A.Ferguson, A.Makena, J.Brem, M.A.Mcdonough, C.J.Schofield. Stucuture of Metallo-Beta-Lactamase To Be Published.