Zinc in PDB 4ubq: Crystal Structure of Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp.

All present enzymatic activity of Crystal Structure of Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp.:
3.5.2.6;

The structure of Crystal Structure of Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp., PDB code: 4ubq was solved by Y.Yamaguchi, S.Matsueda, K.Matsunaga, N.Takashio, S.Toma-Fukai, Y.Yamagata, N.Shibata, J.Wachino, K.Shibayama, Y.Arakawa, H.Kurosaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.16 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.942, 68.488, 88.322, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 29.9

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

Zinc binding site 1 out of 2 in the Crystal Structure of Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp.


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 Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:30.2 occ:1.00 ND1 A:HIS80 2.1 25.4 1.0 NE2 A:HIS140 2.1 24.8 1.0 NE2 A:HIS78 2.2 21.7 1.0 OXT A:ACT303 2.6 27.2 0.5 CD2 A:HIS140 2.9 24.3 1.0 CG A:HIS80 3.1 25.2 1.0 CD2 A:HIS78 3.1 23.3 1.0 CE1 A:HIS80 3.1 25.1 1.0 CE1 A:HIS78 3.2 22.0 1.0 CE1 A:HIS140 3.2 25.7 1.0 CB A:HIS80 3.3 25.3 1.0 C A:ACT303 3.4 27.5 0.5 ZN A:ZN302 3.5 38.2 0.3 OD1 A:ASP82 3.9 32.6 1.0 CH3 A:ACT303 3.9 27.3 0.5 SG A:CYS159 4.0 24.9 0.7 CG A:HIS140 4.2 24.8 1.0 O A:ACT303 4.2 27.6 0.5 CB A:CYS159 4.2 22.6 0.3 SG A:CYS159 4.2 22.0 0.3 NE2 A:HIS80 4.2 22.6 1.0 CD2 A:HIS80 4.2 24.5 1.0 ND1 A:HIS140 4.3 24.9 1.0 CB A:CYS159 4.3 23.0 0.7 CG A:HIS78 4.3 22.6 1.0 ND1 A:HIS78 4.3 22.2 1.0 OD2 A:ASP82 4.4 31.3 1.0 O A:HOH407 4.6 47.2 1.0 CG A:ASP82 4.6 28.7 1.0 CH3 A:ACT303 4.6 21.9 0.5 O A:ACT303 4.7 21.9 0.5 CG2 A:THR141 4.7 23.3 1.0 CA A:HIS80 4.8 25.2 1.0 C A:ACT303 5.0 22.1 0.5

Zinc binding site 2 out of 2 in the Crystal Structure of Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp.


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 Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:38.2 occ:0.30 SG A:CYS159 1.9 24.9 0.7 SG A:CYS159 2.4 22.0 0.3 OD2 A:ASP82 2.5 31.3 1.0 NE2 A:HIS198 2.7 34.9 1.0 CB A:CYS159 3.2 22.6 0.3 O A:ACT303 3.2 21.9 0.5 CB A:CYS159 3.3 23.0 0.7 CH3 A:ACT303 3.3 21.9 0.5 CD2 A:HIS198 3.3 34.7 1.0 ZN A:ZN301 3.5 30.2 1.0 CH3 A:ACT303 3.5 27.3 0.5 CG A:ASP82 3.5 28.7 1.0 C A:ACT303 3.6 27.5 0.5 C A:ACT303 3.6 22.1 0.5 OD1 A:ASP82 3.9 32.6 1.0 CE1 A:HIS198 3.9 34.8 1.0 O A:ACT303 3.9 27.6 0.5 OXT A:ACT303 4.1 27.2 0.5 NE2 A:HIS140 4.2 24.8 1.0 NE2 A:HIS78 4.3 21.7 1.0 CE1 A:HIS78 4.3 22.0 1.0 CB A:SER197 4.3 32.1 1.0 CA A:CYS159 4.4 22.8 0.3 OG A:SER197 4.4 32.5 1.0 CE1 A:HIS140 4.5 25.7 1.0 CA A:CYS159 4.5 23.3 0.7 CG A:HIS198 4.6 34.4 1.0 CD A:LYS34 4.7 26.5 1.0 CE A:LYS34 4.8 26.1 1.0 NZ A:LYS162 4.8 28.1 1.0 CB A:ASP82 4.8 26.2 1.0 ND1 A:HIS198 4.9 34.0 1.0 OXT A:ACT303 4.9 21.9 0.5 CD2 A:HIS140 4.9 24.3 1.0

Y.Yamaguchi, S.Matsueda, K.Matsunaga, N.Takashio, S.Toma-Fukai, Y.Yamagata, N.Shibata, J.Wachino, K.Shibayama, Y.Arakawa, H.Kurosaki. Crystal Structure of Imp-2 Metallo-Beta-Lactamase From Acinetobacter Spp.: Comparison of Active-Site Loop Structures Between Imp-1 and Imp-2 To Be Published.