Zinc in PDB 7fct: Crystal Structure of Metallo-Beta-Lactamase MBLBT2

The structure of Crystal Structure of Metallo-Beta-Lactamase MBLBT2, PDB code: 7fct was solved by F.Zhao, D.H.Peng, T.T.Zou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.76 / 1.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	153.561, 153.561, 53.257, 90, 90, 120
R / Rfree (%)	16.2 / 18.6

The binding sites of Zinc atom in the Crystal Structure of Metallo-Beta-Lactamase MBLBT2 (pdb code 7fct). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Metallo-Beta-Lactamase MBLBT2, PDB code: 7fct:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Metallo-Beta-Lactamase MBLBT2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Metallo-Beta-Lactamase MBLBT2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:7.0 occ:0.70 O A:HOH410 2.0 11.5 1.0 OD2 A:ASP63 2.2 10.4 1.0 NE2 A:HIS64 2.2 12.1 1.0 NE2 A:HIS220 2.2 13.8 1.0 OD2 A:ASP165 2.2 12.0 1.0 CD2 A:HIS64 3.1 10.6 1.0 CD2 A:HIS220 3.1 12.9 1.0 CG A:ASP165 3.1 10.7 1.0 CG A:ASP63 3.2 10.9 1.0 CE1 A:HIS220 3.2 13.3 1.0 ZN A:ZN302 3.3 9.3 0.7 OD1 A:ASP165 3.3 11.5 1.0 CE1 A:HIS64 3.3 10.3 1.0 OD1 A:ASP63 3.5 10.4 1.0 O A:HOH440 4.0 13.8 1.0 CG A:HIS64 4.3 11.1 1.0 CG A:HIS220 4.3 11.4 1.0 NE2 A:HIS59 4.3 11.0 1.0 ND1 A:HIS220 4.3 12.2 1.0 ND1 A:HIS64 4.4 12.3 1.0 CE1 A:HIS59 4.4 11.1 1.0 CB A:ASP63 4.5 10.2 1.0 CB A:ASP165 4.6 11.1 1.0 CE1 A:HIS199 4.6 11.2 1.0 N A:ALA10 4.9 10.9 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Metallo-Beta-Lactamase MBLBT2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Metallo-Beta-Lactamase MBLBT2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:9.3 occ:0.70 O A:HOH410 2.0 11.5 1.0 OD2 A:ASP165 2.2 12.0 1.0 ND1 A:HIS61 2.3 9.5 1.0 NE2 A:HIS142 2.3 9.8 1.0 NE2 A:HIS59 2.3 11.0 1.0 CD2 A:HIS142 3.1 12.2 1.0 CE1 A:HIS61 3.2 12.4 1.0 CD2 A:HIS59 3.2 10.7 1.0 CG A:ASP165 3.3 10.7 1.0 CE1 A:HIS142 3.3 13.4 1.0 ZN A:ZN301 3.3 7.0 0.7 CE1 A:HIS59 3.3 11.1 1.0 CG A:HIS61 3.3 9.9 1.0 CB A:HIS61 3.6 8.4 1.0 CB A:ASP165 3.7 11.1 1.0 NE2 A:HIS64 4.0 12.1 1.0 CD2 A:HIS64 4.0 10.6 1.0 CG A:HIS142 4.3 10.2 1.0 NE2 A:HIS61 4.3 12.1 1.0 OD1 A:ASP165 4.3 11.5 1.0 ND1 A:HIS142 4.3 10.8 1.0 CG A:HIS59 4.4 12.8 1.0 ND1 A:HIS59 4.4 11.5 1.0 CD2 A:HIS61 4.4 10.6 1.0 OD1 A:ASP63 4.5 10.4 1.0 CM B:MPD401 4.5 15.6 1.0 CE1 A:HIS199 4.8 11.2 1.0 OD2 A:ASP63 4.8 10.4 1.0 O2 B:MPD401 4.9 17.1 1.0 CE1 A:HIS64 5.0 10.3 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Metallo-Beta-Lactamase MBLBT2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Metallo-Beta-Lactamase MBLBT2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn404 b:9.0 occ:0.73 O B:HOH523 2.1 12.4 1.0 ND1 B:HIS61 2.3 9.9 1.0 NE2 B:HIS142 2.3 8.8 1.0 NE2 B:HIS59 2.3 10.4 1.0 OD2 B:ASP165 2.3 11.7 1.0 CD2 B:HIS142 3.1 10.3 1.0 CE1 B:HIS61 3.2 11.0 1.0 CD2 B:HIS59 3.2 12.4 1.0 CE1 B:HIS59 3.3 10.1 1.0 CE1 B:HIS142 3.3 9.8 1.0 CG B:ASP165 3.3 10.1 1.0 CG B:HIS61 3.3 10.7 1.0 ZN B:ZN405 3.3 8.4 0.7 CB B:HIS61 3.6 9.2 1.0 CB B:ASP165 3.7 9.0 1.0 NE2 B:HIS64 4.0 10.3 1.0 CD2 B:HIS64 4.0 9.1 1.0 CG B:HIS142 4.3 12.2 1.0 ND1 B:HIS142 4.3 10.8 1.0 NE2 B:HIS61 4.3 10.6 1.0 OD1 B:ASP165 4.3 10.3 1.0 CG B:HIS59 4.3 10.3 1.0 ND1 B:HIS59 4.4 10.1 1.0 OD1 B:ASP63 4.4 11.1 1.0 CD2 B:HIS61 4.4 9.1 1.0 C1 B:MPD402 4.6 19.6 1.0 CE1 B:HIS199 4.8 11.0 1.0 OD2 B:ASP63 4.8 9.9 1.0 O2 B:MPD402 5.0 19.8 1.0 CE1 B:HIS64 5.0 10.3 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Metallo-Beta-Lactamase MBLBT2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Metallo-Beta-Lactamase MBLBT2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn405 b:8.4 occ:0.70 O B:HOH523 2.0 12.4 1.0 OD2 B:ASP63 2.2 9.9 1.0 NE2 B:HIS64 2.2 10.3 1.0 NE2 B:HIS220 2.2 11.0 1.0 OD2 B:ASP165 2.3 11.7 1.0 CD2 B:HIS64 3.0 9.1 1.0 CG B:ASP63 3.1 10.4 1.0 CG B:ASP165 3.1 10.1 1.0 CD2 B:HIS220 3.1 11.5 1.0 CE1 B:HIS220 3.2 10.2 1.0 OD1 B:ASP165 3.3 10.3 1.0 CE1 B:HIS64 3.3 10.3 1.0 ZN B:ZN404 3.3 9.0 0.7 OD1 B:ASP63 3.4 11.1 1.0 O B:HOH564 3.9 11.6 1.0 CG B:HIS64 4.3 8.8 1.0 CG B:HIS220 4.3 9.6 1.0 ND1 B:HIS220 4.3 11.1 1.0 NE2 B:HIS59 4.3 10.4 1.0 ND1 B:HIS64 4.3 10.5 1.0 CE1 B:HIS59 4.4 10.1 1.0 CB B:ASP63 4.5 9.6 1.0 CB B:ASP165 4.5 9.0 1.0 CE1 B:HIS199 4.6 11.0 1.0 N B:ALA10 4.8 11.9 1.0

F.Zhao, D.H.Peng, T.T.Zou. Crystal Structure of Metallo-Beta-Lactamase MBLBT2 To Be Published.