Zinc in PDB 7zo7: L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole

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

The structure of L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole, PDB code: 7zo7 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)	66.86 / 1.63
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.469, 105.469, 98.135, 90, 90, 120
R / Rfree (%)	15.9 / 17.5

The binding sites of Zinc atom in the L1 Metallo-Beta-Lactamase in Complex with Hydrolysed Cefmetazole (pdb code 7zo7). 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 Cefmetazole, PDB code: 7zo7:
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 Cefmetazole


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 Cefmetazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:21.8 occ:1.00 O A:HOH411 1.9 26.2 1.0 NE2 A:HIS160 2.0 19.0 1.0 NE2 A:HIS84 2.1 19.9 1.0 ND1 A:HIS86 2.1 22.0 1.0 O19 A:JOU304 2.5 31.9 1.0 CD2 A:HIS160 2.9 18.7 1.0 HD2 A:HIS160 3.0 22.5 1.0 CD2 A:HIS84 3.0 20.2 1.0 CE1 A:HIS86 3.0 21.4 1.0 CE1 A:HIS84 3.0 21.3 1.0 HB2 A:HIS86 3.0 23.8 1.0 CG A:HIS86 3.1 19.7 1.0 CE1 A:HIS160 3.1 23.1 1.0 HE1 A:HIS86 3.2 25.7 1.0 HD2 A:HIS84 3.2 24.2 1.0 HE1 A:HIS84 3.2 25.5 1.0 H173 A:JOU304 3.3 46.8 1.0 HE1 A:HIS160 3.4 27.8 1.0 O03 A:JOU304 3.4 24.9 1.0 CB A:HIS86 3.5 19.8 1.0 HD2 A:HIS89 3.5 28.1 1.0 HB3 A:HIS86 3.6 23.8 1.0 ZN A:ZN302 3.7 25.8 1.0 C18 A:JOU304 3.7 51.4 1.0 ND1 A:HIS84 4.1 20.2 1.0 CG A:HIS160 4.1 20.6 1.0 N05 A:JOU304 4.1 32.7 1.0 CG A:HIS84 4.1 19.1 1.0 NE2 A:HIS86 4.1 21.2 1.0 OD1 A:ASP88 4.2 23.0 1.0 ND1 A:HIS160 4.2 20.5 1.0 C02 A:JOU304 4.2 30.6 1.0 C17 A:JOU304 4.2 39.0 1.0 CD2 A:HIS86 4.2 19.4 1.0 O16 A:JOU304 4.2 41.6 1.0 CD2 A:HIS89 4.2 23.4 1.0 HG23 A:THR161 4.4 24.0 1.0 NE2 A:HIS89 4.4 26.1 1.0 HE2 A:PHE124 4.4 54.4 1.0 HG A:SER185 4.4 21.7 0.6 C04 A:JOU304 4.4 33.6 1.0 C07 A:JOU304 4.5 52.7 1.0 O20 A:JOU304 4.7 55.5 1.0 H172 A:JOU304 4.8 46.8 1.0 HB3 A:SER185 4.8 26.2 0.4 HB2 A:SER185 4.9 25.9 0.6 HD1 A:HIS84 4.9 24.3 1.0 H171 A:JOU304 4.9 46.8 1.0 H A:HIS86 4.9 22.1 1.0 HE2 A:HIS86 4.9 25.4 1.0 CA A:HIS86 4.9 19.3 1.0 OD2 A:ASP88 4.9 25.8 1.0 HD1 A:HIS160 5.0 24.6 1.0 HG21 A:THR161 5.0 24.0 1.0 CG A:ASP88 5.0 26.7 1.0

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


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 Cefmetazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:25.8 occ:1.00 NE2 A:HIS225 2.1 24.5 1.0 NE2 A:HIS89 2.1 26.1 1.0 OD2 A:ASP88 2.2 25.8 1.0 O A:HOH411 2.2 26.2 1.0 O03 A:JOU304 2.2 24.9 1.0 N05 A:JOU304 2.4 32.7 1.0 CD2 A:HIS225 3.0 23.8 1.0 CG A:ASP88 3.0 26.7 1.0 CE1 A:HIS89 3.0 26.9 1.0 CD2 A:HIS89 3.1 23.4 1.0 C02 A:JOU304 3.1 30.6 1.0 CE1 A:HIS225 3.1 25.6 1.0 HD2 A:HIS225 3.1 28.6 1.0 HE1 A:HIS89 3.2 32.2 1.0 C04 A:JOU304 3.2 33.6 1.0 OD1 A:ASP88 3.3 23.0 1.0 HD2 A:HIS89 3.3 28.1 1.0 HE1 A:HIS225 3.3 30.7 1.0 H061 A:JOU304 3.4 71.3 1.0 C06 A:JOU304 3.5 59.4 1.0 HE1 A:HIS84 3.6 25.5 1.0 ZN A:ZN301 3.7 21.8 1.0 HG A:SER185 3.8 21.7 0.6 O16 A:JOU304 3.9 41.6 1.0 O19 A:JOU304 4.1 31.9 1.0 ND1 A:HIS89 4.1 22.9 1.0 CG A:HIS225 4.2 25.6 1.0 ND1 A:HIS225 4.2 25.3 1.0 CG A:HIS89 4.2 21.2 1.0 C07 A:JOU304 4.2 52.7 1.0 O01 A:JOU304 4.2 28.6 1.0 CE1 A:HIS84 4.2 21.3 1.0 NE2 A:HIS84 4.3 19.9 1.0 H242 A:JOU304 4.3 75.9 1.0 CB A:ASP88 4.4 20.0 1.0 HB2 A:ASP88 4.4 24.0 1.0 C18 A:JOU304 4.4 51.4 1.0 H241 A:JOU304 4.5 75.9 1.0 OG A:SER185 4.5 18.1 0.6 C23 A:JOU304 4.6 41.6 1.0 C24 A:JOU304 4.7 63.3 1.0 HH2 A:TRP17 4.8 33.7 1.0 NE2 A:HIS160 4.8 19.0 1.0 H173 A:JOU304 4.8 46.8 1.0 HB2 A:PRO224 4.8 25.6 1.0 S21 A:JOU304 4.9 35.8 1.0 HB2 A:HIS86 4.9 23.8 1.0 HB2 A:SER185 4.9 26.2 0.4 HB3 A:ASP88 4.9 24.0 1.0 HD1 A:HIS89 4.9 27.4 1.0 HZ3 A:TRP17 4.9 30.2 1.0 C17 A:JOU304 4.9 39.0 1.0 HD1 A:HIS225 5.0 30.4 1.0

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