Zinc in PDB 7zo4: L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem

All present enzymatic activity of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem:
3.5.2.6;

The structure of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem, PDB code: 7zo4 was solved by P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.82 / 1.43
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.081, 105.081, 98.418, 90, 90, 120
R / Rfree (%)	16.3 / 20

The structure of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Zinc atom in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem (pdb code 7zo4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem, PDB code: 7zo4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:29.0 occ:1.00 O A:HOH451 2.0 26.6 1.0 OD2 A:ASP88 2.2 27.8 1.0 N14 A:JOI306 2.2 32.0 1.0 NE2 A:HIS89 2.2 26.5 1.0 NE2 A:HIS225 2.2 28.2 1.0 O24 A:JOI306 2.3 28.5 1.0 C03 A:JOI306 3.0 32.2 1.0 CG A:ASP88 3.0 26.8 1.0 C02 A:JOI306 3.1 30.4 1.0 CD2 A:HIS89 3.2 26.1 1.0 CD2 A:HIS225 3.2 31.1 1.0 CE1 A:HIS89 3.2 27.4 1.0 CE1 A:HIS225 3.2 28.6 1.0 OD1 A:ASP88 3.3 25.3 1.0 HD2 A:HIS225 3.3 37.4 1.0 H171 A:JOI306 3.3 38.3 1.0 HD2 A:HIS89 3.3 31.4 1.0 HE1 A:HIS89 3.4 32.9 1.0 C15 A:JOI306 3.4 30.4 1.0 HE1 A:HIS225 3.4 34.3 1.0 ZN A:ZN302 3.6 27.4 1.0 H151 A:JOI306 3.7 46.8 1.0 O22 A:JOI306 3.8 30.5 1.0 C17 A:JOI306 3.8 30.5 1.0 HG A:SER185 3.9 33.7 1.0 HE1 A:HIS84 4.0 31.9 1.0 ND1 A:HIS89 4.3 27.3 1.0 O01 A:JOI306 4.3 29.7 1.0 CG A:HIS89 4.3 26.0 1.0 H061 A:JOI306 4.3 48.8 1.0 ND1 A:HIS225 4.3 29.5 1.0 CG A:HIS225 4.3 30.2 1.0 CB A:ASP88 4.4 25.7 1.0 HB2 A:ASP88 4.4 30.8 1.0 C04 A:JOI306 4.4 33.1 1.0 NE2 A:HIS84 4.4 25.6 1.0 C21 A:JOI306 4.5 33.0 1.0 CE1 A:HIS84 4.5 26.6 1.0 H221 A:JOI306 4.6 40.1 1.0 C16 A:JOI306 4.6 34.9 1.0 OG A:SER185 4.7 28.1 1.0 H231 A:JOI306 4.7 44.6 1.0 NE2 A:HIS160 4.7 27.7 1.0 HZ3 A:TRP17 4.8 35.5 1.0 HH2 A:TRP17 4.8 38.8 1.0 HB3 A:ASP88 4.9 30.8 1.0 HB2 A:HIS86 4.9 29.6 1.0 HE1 A:HIS160 4.9 34.0 1.0 HB2 A:PRO224 4.9 31.2 1.0

Zinc binding site 2 out of 2 in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:27.4 occ:1.00 O A:HOH451 1.8 26.6 1.0 NE2 A:HIS160 2.1 27.7 1.0 NE2 A:HIS84 2.1 25.6 1.0 ND1 A:HIS86 2.2 24.9 1.0 HB2 A:HIS86 2.9 29.6 1.0 CD2 A:HIS160 2.9 27.9 1.0 HD2 A:HIS160 3.0 33.5 1.0 CE1 A:HIS84 3.1 26.6 1.0 CD2 A:HIS84 3.1 26.5 1.0 CG A:HIS86 3.1 25.3 1.0 CE1 A:HIS86 3.2 25.0 1.0 CE1 A:HIS160 3.3 28.4 1.0 HE1 A:HIS84 3.3 31.9 1.0 HD2 A:HIS84 3.3 31.8 1.0 H221 A:JOI306 3.3 40.1 1.0 HD2 A:HIS89 3.3 31.4 1.0 O22 A:JOI306 3.3 30.5 1.0 HE1 A:HIS86 3.4 29.9 1.0 CB A:HIS86 3.4 24.6 1.0 O24 A:JOI306 3.5 28.5 1.0 HE1 A:HIS160 3.5 34.0 1.0 ZN A:ZN301 3.6 29.0 1.0 HB3 A:HIS86 3.6 29.6 1.0 CD2 A:HIS89 4.0 26.1 1.0 H231 A:JOI306 4.1 44.6 1.0 OD1 A:ASP88 4.1 25.3 1.0 ND1 A:HIS84 4.1 25.9 1.0 CG A:HIS160 4.2 25.6 1.0 CG A:HIS84 4.2 25.8 1.0 NE2 A:HIS89 4.2 26.5 1.0 C02 A:JOI306 4.2 30.4 1.0 ND1 A:HIS160 4.3 27.1 1.0 NE2 A:HIS86 4.3 26.1 1.0 CD2 A:HIS86 4.3 25.9 1.0 HE2 A:PHE124 4.3 46.7 1.0 N14 A:JOI306 4.4 32.0 1.0 HG A:SER185 4.4 33.7 1.0 HG23 A:THR161 4.4 29.1 1.0 C03 A:JOI306 4.4 32.2 1.0 C21 A:JOI306 4.6 33.0 1.0 C23 A:JOI306 4.8 36.0 1.0 H A:HIS86 4.8 27.8 1.0 OD2 A:ASP88 4.8 27.8 1.0 CA A:HIS86 4.9 22.7 1.0 HB2 A:SER185 4.9 32.5 1.0 CG A:ASP88 4.9 26.8 1.0 HD1 A:HIS84 4.9 31.1 1.0 H171 A:JOI306 4.9 38.3 1.0

P.Hinchliffe, J.Spencer. L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Panipenem To Be Published.