Zinc in PDB 7zo6: L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefoxitin

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

The structure of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefoxitin, PDB code: 7zo6 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)	45.62 / 1.61
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.345, 105.345, 97.891, 90, 90, 120
R / Rfree (%)	16.4 / 18.8

The binding sites of Zinc atom in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefoxitin (pdb code 7zo6). 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 Cefoxitin, PDB code: 7zo6:
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 Cefoxitin


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 Cefoxitin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:34.8 occ:1.00 OD2 A:ASP88 2.1 34.6 1.0 O A:HOH401 2.1 31.9 1.0 NE2 A:HIS89 2.2 32.2 1.0 N05 A:JNX304 2.2 41.1 0.3 NE2 A:HIS225 2.2 34.1 1.0 N05 A:JNX304 2.2 41.1 0.7 O03 A:JNX304 2.2 37.0 0.7 O03 A:JNX304 2.4 36.8 0.3 C04 A:JNX304 2.9 38.4 0.3 C04 A:JNX304 2.9 38.0 0.7 C02 A:JNX304 3.0 39.1 0.7 CG A:ASP88 3.0 38.0 1.0 C02 A:JNX304 3.0 39.1 0.3 CD2 A:HIS89 3.1 29.0 1.0 CE1 A:HIS89 3.1 36.4 1.0 CD2 A:HIS225 3.1 36.1 1.0 CE1 A:HIS225 3.2 36.7 1.0 OD1 A:ASP88 3.3 32.2 1.0 HD2 A:HIS225 3.3 43.4 1.0 HD2 A:HIS89 3.3 34.8 1.0 C06 A:JNX304 3.3 43.1 0.3 HE1 A:HIS89 3.3 43.6 1.0 C06 A:JNX304 3.4 42.8 0.7 HE1 A:HIS225 3.4 44.0 1.0 H061 A:JNX304 3.5 51.7 0.3 H061 A:JNX304 3.6 51.3 0.7 ZN A:ZN302 3.6 31.6 1.0 O20 A:JNX304 3.7 41.9 0.3 HE1 A:HIS84 3.7 38.7 1.0 HG A:SER185 3.8 41.0 1.0 O17 A:JNX304 3.8 43.3 0.7 O17 A:JNX304 3.9 43.7 0.3 O20 A:JNX304 3.9 41.4 0.7 C07 A:JNX304 4.0 47.3 0.3 C07 A:JNX304 4.0 47.3 0.7 O01 A:JNX304 4.2 37.7 0.7 ND1 A:HIS89 4.2 29.7 1.0 CG A:HIS89 4.2 31.0 1.0 C19 A:JNX304 4.2 50.0 0.3 O01 A:JNX304 4.2 37.8 0.3 CG A:HIS225 4.3 36.8 1.0 NE2 A:HIS84 4.3 32.3 1.0 ND1 A:HIS225 4.3 36.6 1.0 CE1 A:HIS84 4.3 32.2 1.0 C19 A:JNX304 4.3 50.4 0.7 CB A:ASP88 4.4 32.4 1.0 HB2 A:ASP88 4.4 38.9 1.0 C24 A:JNX304 4.5 41.9 0.3 C24 A:JNX304 4.5 41.4 0.7 OG A:SER185 4.5 34.2 1.0 H251 A:JNX304 4.6 63.8 0.7 H252 A:JNX304 4.6 63.8 0.7 H251 A:JNX304 4.7 63.7 0.3 H252 A:JNX304 4.7 63.7 0.3 HH2 A:TRP17 4.8 49.8 1.0 NE2 A:HIS160 4.8 29.0 1.0 HB2 A:HIS86 4.8 38.4 1.0 S22 A:JNX304 4.8 42.0 0.7 HB2 A:PRO224 4.8 38.4 1.0 C25 A:JNX304 4.8 53.2 0.7 S22 A:JNX304 4.9 42.9 0.3 HB3 A:ASP88 4.9 38.9 1.0 C25 A:JNX304 4.9 53.1 0.3 HD1 A:HIS89 5.0 35.6 1.0

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


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 Cefoxitin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:31.6 occ:1.00 O A:HOH401 1.9 31.9 1.0 NE2 A:HIS160 2.2 29.0 1.0 NE2 A:HIS84 2.2 32.3 1.0 ND1 A:HIS86 2.2 29.9 1.0 O20 A:JNX304 2.3 41.9 0.3 O20 A:JNX304 2.4 41.4 0.7 CD2 A:HIS160 2.9 27.8 1.0 HB2 A:HIS86 3.0 38.4 1.0 HD2 A:HIS160 3.0 33.3 1.0 CE1 A:HIS84 3.1 32.2 1.0 CD2 A:HIS84 3.1 32.1 1.0 CG A:HIS86 3.1 31.7 1.0 CE1 A:HIS86 3.2 32.3 1.0 CE1 A:HIS160 3.3 32.5 1.0 HD2 A:HIS84 3.3 38.5 1.0 HE1 A:HIS84 3.3 38.7 1.0 HE1 A:HIS86 3.4 38.7 1.0 O03 A:JNX304 3.4 37.0 0.7 CB A:HIS86 3.4 32.0 1.0 O03 A:JNX304 3.4 36.8 0.3 HD2 A:HIS89 3.5 34.8 1.0 C19 A:JNX304 3.6 50.0 0.3 HB3 A:HIS86 3.6 38.4 1.0 HE1 A:HIS160 3.6 39.0 1.0 ZN A:ZN301 3.6 34.8 1.0 C19 A:JNX304 3.6 50.4 0.7 H183 A:JNX304 3.9 54.0 0.3 H183 A:JNX304 3.9 54.0 0.7 C02 A:JNX304 4.1 39.1 0.7 C02 A:JNX304 4.1 39.1 0.3 OD1 A:ASP88 4.1 32.2 1.0 O17 A:JNX304 4.1 43.3 0.7 ND1 A:HIS84 4.2 31.2 1.0 CG A:HIS160 4.2 28.5 1.0 O17 A:JNX304 4.2 43.7 0.3 N05 A:JNX304 4.2 41.1 0.7 CD2 A:HIS89 4.2 29.0 1.0 CG A:HIS84 4.2 31.3 1.0 N05 A:JNX304 4.2 41.1 0.3 HE2 A:PHE124 4.2 59.7 1.0 NE2 A:HIS86 4.3 31.1 1.0 CD2 A:HIS86 4.3 27.4 1.0 ND1 A:HIS160 4.3 30.0 1.0 HG A:SER185 4.3 41.0 1.0 NE2 A:HIS89 4.4 32.2 1.0 HG23 A:THR161 4.4 34.2 1.0 C18 A:JNX304 4.4 45.0 0.7 C18 A:JNX304 4.4 45.0 0.3 C04 A:JNX304 4.4 38.0 0.7 C07 A:JNX304 4.4 47.3 0.3 C07 A:JNX304 4.5 47.3 0.7 C04 A:JNX304 4.5 38.4 0.3 O21 A:JNX304 4.5 49.8 0.3 H181 A:JNX304 4.5 54.0 0.7 H181 A:JNX304 4.5 54.0 0.3 O21 A:JNX304 4.6 49.7 0.7 OD2 A:ASP88 4.8 34.6 1.0 HB2 A:SER185 4.9 42.5 1.0 H A:HIS86 4.9 34.8 1.0 CA A:HIS86 4.9 28.5 1.0 CG A:ASP88 4.9 38.0 1.0 HD1 A:HIS84 4.9 37.5 1.0 O01 A:JNX304 5.0 37.7 0.7

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