Zinc in PDB 7zo3: L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Tebipenem

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

The structure of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Tebipenem, PDB code: 7zo3 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)	66.83 / 1.43
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.274, 105.274, 98.241, 90, 90, 120
R / Rfree (%)	17.3 / 19.7

The binding sites of Zinc atom in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Tebipenem (pdb code 7zo3). 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 Tebipenem, PDB code: 7zo3:
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 Tebipenem


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 Tebipenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:29.0 occ:1.00 OD2 A:ASP88 2.0 29.6 1.0 N15 A:JNQ306 2.0 28.7 1.0 NE2 A:HIS89 2.2 26.7 1.0 NE2 A:HIS225 2.2 26.6 1.0 O01 A:JNQ306 2.4 27.8 1.0 O22 A:JNQ306 2.8 33.0 1.0 C03 A:JNQ306 2.9 27.6 1.0 CG A:ASP88 2.9 29.9 1.0 CE1 A:HIS89 3.0 26.6 1.0 C02 A:JNQ306 3.1 26.6 1.0 CD2 A:HIS225 3.1 25.8 1.0 HE1 A:HIS89 3.1 31.9 1.0 CD2 A:HIS89 3.1 25.5 1.0 OD1 A:ASP88 3.2 27.2 1.0 CE1 A:HIS225 3.2 27.9 1.0 C16 A:JNQ306 3.2 33.6 1.0 HD2 A:HIS225 3.3 31.0 1.0 HE1 A:HIS225 3.4 33.5 1.0 H231 A:JNQ306 3.4 39.2 1.0 HD2 A:HIS89 3.4 30.6 1.0 H161 A:JNQ306 3.4 46.6 1.0 C20 A:JNQ306 3.5 32.9 1.0 C19 A:JNQ306 3.7 28.6 1.0 HE1 A:HIS84 3.9 31.5 1.0 HG A:SER185 4.0 33.2 1.0 ZN A:ZN302 4.1 26.6 1.0 C23 A:JNQ306 4.1 31.9 1.0 ND1 A:HIS89 4.1 26.2 1.0 CG A:HIS89 4.2 26.7 1.0 ND1 A:HIS225 4.3 30.1 1.0 CG A:HIS225 4.3 30.4 1.0 CB A:ASP88 4.3 28.1 1.0 C04 A:JNQ306 4.3 30.3 1.0 O26 A:JNQ306 4.3 28.4 1.0 HB2 A:ASP88 4.3 33.8 1.0 C17 A:JNQ306 4.3 28.8 1.0 O21 A:JNQ306 4.5 28.3 1.0 CE1 A:HIS84 4.5 26.2 1.0 NE2 A:HIS84 4.5 25.5 1.0 HZ3 A:TRP17 4.5 33.6 1.0 HH2 A:TRP17 4.6 39.2 1.0 H171 A:JNQ306 4.6 42.8 1.0 HD21 A:LEU38 4.7 34.0 1.0 OG A:SER185 4.8 27.6 1.0 HB3 A:ASP88 4.8 33.8 1.0 H191 A:JNQ306 4.8 43.2 1.0 HB2 A:PRO224 4.8 29.5 1.0 HD1 A:HIS89 4.9 31.5 1.0 H041 A:JNQ306 4.9 41.4 1.0 CZ3 A:TRP17 4.9 27.9 1.0 CH2 A:TRP17 4.9 32.6 1.0 HD22 A:LEU38 4.9 34.0 1.0 O24 A:JNQ306 5.0 35.7 1.0 HB2 A:HIS86 5.0 28.3 1.0

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


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 Tebipenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:26.6 occ:1.00 O22 A:JNQ306 1.9 33.0 1.0 NE2 A:HIS160 2.1 26.1 1.0 ND1 A:HIS86 2.1 25.5 1.0 NE2 A:HIS84 2.2 25.5 1.0 C20 A:JNQ306 2.6 32.9 1.0 O21 A:JNQ306 2.6 28.3 1.0 CD2 A:HIS160 3.0 25.3 1.0 HB2 A:HIS86 3.0 28.3 1.0 CD2 A:HIS84 3.0 23.6 1.0 HD2 A:HIS160 3.1 30.5 1.0 CE1 A:HIS84 3.1 26.2 1.0 CE1 A:HIS86 3.1 26.7 1.0 CG A:HIS86 3.1 25.2 1.0 CE1 A:HIS160 3.2 24.1 1.0 HD2 A:HIS84 3.2 28.4 1.0 HE1 A:HIS86 3.3 32.1 1.0 HE1 A:HIS84 3.3 31.5 1.0 HE1 A:HIS160 3.4 29.1 1.0 CB A:HIS86 3.4 23.5 1.0 HD2 A:HIS89 3.6 30.6 1.0 HB3 A:HIS86 3.6 28.3 1.0 O01 A:JNQ306 3.7 27.8 1.0 ZN A:ZN301 4.1 29.0 1.0 C19 A:JNQ306 4.1 28.6 1.0 ND1 A:HIS84 4.1 24.4 1.0 CG A:HIS84 4.1 24.2 1.0 CG A:HIS160 4.2 24.5 1.0 H253 A:JNQ306 4.2 44.0 1.0 HE2 A:PHE124 4.2 39.5 1.0 NE2 A:HIS86 4.2 25.0 1.0 ND1 A:HIS160 4.2 26.8 1.0 CD2 A:HIS86 4.2 22.9 1.0 C02 A:JNQ306 4.2 26.6 1.0 N15 A:JNQ306 4.2 28.7 1.0 CD2 A:HIS89 4.3 25.5 1.0 HG23 A:THR161 4.3 29.6 1.0 OD1 A:ASP88 4.4 27.2 1.0 C03 A:JNQ306 4.4 27.6 1.0 NE2 A:HIS89 4.5 26.7 1.0 H231 A:JNQ306 4.5 39.2 1.0 H252 A:JNQ306 4.5 44.0 1.0 HG A:SER185 4.6 33.2 1.0 C23 A:JNQ306 4.7 31.9 1.0 C25 A:JNQ306 4.7 32.7 1.0 HZ A:PHE124 4.7 38.2 1.0 H191 A:JNQ306 4.7 43.2 1.0 HB2 A:SER185 4.8 31.9 1.0 H A:HIS86 4.8 28.6 1.0 C16 A:JNQ306 4.9 33.6 1.0 HD1 A:HIS84 4.9 29.4 1.0 H041 A:JNQ306 4.9 41.4 1.0 CA A:HIS86 4.9 23.1 1.0 HG21 A:THR161 4.9 29.6 1.0 CG2 A:THR161 5.0 24.6 1.0 HG22 A:THR161 5.0 29.6 1.0 CE2 A:PHE124 5.0 32.9 1.0 HE2 A:HIS86 5.0 30.1 1.0

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