Zinc in PDB 1a7t: Metallo-Beta-Lactamase with Mes

All present enzymatic activity of Metallo-Beta-Lactamase with Mes:
3.5.2.6;

The structure of Metallo-Beta-Lactamase with Mes, PDB code: 1a7t was solved by P.M.D.Fitzgerald, J.K.Wu, J.H.Toney, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.270, 66.960, 69.480, 90.00, 103.77, 90.00
R / Rfree (%)	n/a / n/a

The structure of Metallo-Beta-Lactamase with Mes also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Zinc atom in the Metallo-Beta-Lactamase with Mes (pdb code 1a7t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Metallo-Beta-Lactamase with Mes, PDB code: 1a7t:
Jump to Zinc binding site number: 1; 2; 3; 4;

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


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 with Mes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn251 b:10.2 occ:1.00 O A:HOH256 1.9 7.8 1.0 ND1 A:HIS84 2.0 8.1 1.0 NE2 A:HIS145 2.1 7.8 1.0 NE2 A:HIS82 2.1 7.4 1.0 CE1 A:HIS84 2.9 6.7 1.0 CD2 A:HIS145 3.0 6.9 1.0 CE1 A:HIS82 3.0 7.0 1.0 CE1 A:HIS145 3.1 7.0 1.0 CG A:HIS84 3.1 7.1 1.0 CD2 A:HIS82 3.1 6.7 1.0 O A:HOH280 3.4 16.1 1.0 CB A:HIS84 3.5 7.5 1.0 ZN A:ZN252 3.5 13.3 1.0 OD1 A:ASP86 3.9 8.0 1.0 O A:HOH257 4.0 8.7 1.0 NE2 A:HIS84 4.0 6.8 1.0 CD2 A:HIS84 4.1 7.6 1.0 ND1 A:HIS145 4.1 7.7 1.0 CG A:HIS145 4.1 7.1 1.0 ND1 A:HIS82 4.2 7.0 1.0 CG A:HIS82 4.2 6.8 1.0 CB A:CYS164 4.2 6.5 1.0 SG A:CYS164 4.3 7.6 1.0 OD2 A:ASP86 4.5 7.9 1.0 CG A:ASP86 4.7 8.0 1.0 CA A:HIS84 4.8 7.4 1.0 O A:HOH336 5.0 35.0 1.0

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


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 with Mes within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn252 b:13.3 occ:1.00 O A:HOH256 2.1 7.8 1.0 SG A:CYS164 2.2 7.6 1.0 NE2 A:HIS206 2.2 10.5 1.0 OD2 A:ASP86 2.3 7.9 1.0 O A:HOH257 2.3 8.7 1.0 CD2 A:HIS206 3.1 10.7 1.0 CE1 A:HIS206 3.2 10.7 1.0 CG A:ASP86 3.3 8.0 1.0 CB A:CYS164 3.3 6.5 1.0 ZN A:ZN251 3.5 10.2 1.0 OD1 A:ASP86 3.5 8.0 1.0 O A:HOH266 3.8 10.5 1.0 NE2 A:HIS145 4.2 7.8 1.0 O A:HOH280 4.2 16.1 1.0 CG A:HIS206 4.3 10.4 1.0 ND1 A:HIS206 4.3 10.8 1.0 CE1 A:HIS82 4.3 7.0 1.0 O1S A:MES250 4.4 28.9 1.0 NE2 A:HIS82 4.4 7.4 1.0 CE1 A:HIS145 4.4 7.0 1.0 O A:HOH272 4.5 13.2 1.0 CA A:CYS164 4.6 7.5 1.0 CB A:ASP86 4.6 7.6 1.0 C5 A:MES250 4.6 27.7 1.0 CD2 A:HIS145 4.9 6.9 1.0 C7 A:MES250 4.9 28.6 1.0 N4 A:MES250 5.0 28.1 1.0 CA A:GLY205 5.0 7.7 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Metallo-Beta-Lactamase with Mes within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn251 b:9.5 occ:1.00 O B:HOH256 1.9 5.1 1.0 NE2 B:HIS145 2.1 5.6 1.0 ND1 B:HIS84 2.1 5.7 1.0 NE2 B:HIS82 2.1 6.5 1.0 CD2 B:HIS145 2.9 5.4 1.0 CG B:HIS84 3.0 6.2 1.0 CE1 B:HIS82 3.0 5.4 1.0 CE1 B:HIS84 3.1 6.3 1.0 CE1 B:HIS145 3.1 5.0 1.0 CD2 B:HIS82 3.1 5.0 1.0 CB B:HIS84 3.3 5.5 1.0 O B:HOH282 3.5 16.9 1.0 ZN B:ZN252 3.5 11.3 1.0 O B:HOH257 3.9 8.1 1.0 OD1 B:ASP86 4.0 7.4 1.0 CG B:HIS145 4.1 5.9 1.0 NE2 B:HIS84 4.2 6.5 1.0 ND1 B:HIS82 4.2 5.4 1.0 CD2 B:HIS84 4.2 6.5 1.0 ND1 B:HIS145 4.2 5.6 1.0 CG B:HIS82 4.2 4.5 1.0 CB B:CYS164 4.3 6.7 1.0 SG B:CYS164 4.3 7.3 1.0 OD2 B:ASP86 4.4 7.1 1.0 CG B:ASP86 4.7 7.3 1.0 CA B:HIS84 4.8 6.0 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Metallo-Beta-Lactamase with Mes within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn252 b:11.3 occ:1.00 O B:HOH257 2.2 8.1 1.0 OD2 B:ASP86 2.2 7.1 1.0 O B:HOH256 2.2 5.1 1.0 NE2 B:HIS206 2.2 7.0 1.0 SG B:CYS164 2.3 7.3 1.0 CD2 B:HIS206 3.1 6.9 1.0 CG B:ASP86 3.2 7.3 1.0 CE1 B:HIS206 3.2 6.5 1.0 CB B:CYS164 3.3 6.7 1.0 ZN B:ZN251 3.5 9.5 1.0 OD1 B:ASP86 3.6 7.4 1.0 O B:HOH263 3.9 7.9 1.0 NE2 B:HIS145 4.2 5.6 1.0 O B:HOH282 4.2 16.9 1.0 C5 B:MES250 4.2 25.0 1.0 CG B:HIS206 4.2 7.0 1.0 ND1 B:HIS206 4.3 7.4 1.0 CE1 B:HIS82 4.4 5.4 1.0 CE1 B:HIS145 4.5 5.0 1.0 NE2 B:HIS82 4.5 6.5 1.0 O B:HOH266 4.5 9.3 1.0 O1S B:MES250 4.6 29.9 1.0 CB B:ASP86 4.6 6.2 1.0 CA B:CYS164 4.6 6.7 1.0 N4 B:MES250 4.8 25.7 1.0 C7 B:MES250 4.8 26.5 1.0 CD2 B:HIS145 4.9 5.4 1.0 C6 B:MES250 4.9 24.8 1.0

P.M.Fitzgerald, J.K.Wu, J.H.Toney. Unanticipated Inhibition of the Metallo-Beta-Lactamase From Bacteroides Fragilis By 4-Morpholineethanesulfonic Acid (Mes): A Crystallographic Study at 1.85-A Resolution. Biochemistry V. 37 6791 1998.
ISSN: ISSN 0006-2960
PubMed: 9578564
DOI: 10.1021/BI9730339