Zinc in PDB 7o0o: Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem

All present enzymatic activity of Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem:
3.5.2.6;

The structure of Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem, PDB code: 7o0o 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)	32.72 / 1.45
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.803, 105.803, 98.149, 90, 90, 120
R / Rfree (%)	15.4 / 16.9

The binding sites of Zinc atom in the Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem (pdb code 7o0o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem, PDB code: 7o0o:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem


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 the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:16.3 occ:1.00 O6 A:LHT304 2.0 33.8 1.0 NE2 A:HIS160 2.0 15.4 1.0 ND1 A:HIS86 2.1 14.8 1.0 NE2 A:HIS84 2.1 15.0 1.0 C20 A:LHT304 2.6 45.0 1.0 O7 A:LHT304 2.8 26.4 1.0 CD2 A:HIS160 3.0 14.2 1.0 CD2 A:HIS84 3.0 13.6 1.0 CE1 A:HIS86 3.0 15.5 1.0 CE1 A:HIS84 3.0 17.4 1.0 HB2 A:HIS86 3.0 15.4 1.0 CE1 A:HIS160 3.1 16.5 1.0 HD2 A:HIS160 3.1 17.0 1.0 CG A:HIS86 3.1 13.6 1.0 HE1 A:HIS86 3.2 18.6 1.0 HD2 A:HIS84 3.2 16.3 1.0 HE1 A:HIS84 3.2 20.9 1.0 HE1 A:HIS160 3.3 19.8 1.0 CB A:HIS86 3.5 12.9 1.0 HD2 A:HIS89 3.6 19.4 1.0 HB3 A:HIS86 3.6 15.4 1.0 O5 A:LHT304 3.6 27.3 1.0 ZN A:ZN302 3.9 20.6 1.0 ND1 A:HIS84 4.1 16.4 1.0 CG A:HIS84 4.1 13.6 1.0 CG A:HIS160 4.1 14.7 1.0 NE2 A:HIS86 4.1 14.8 1.0 ND1 A:HIS160 4.1 16.6 1.0 C19 A:LHT304 4.2 38.7 1.0 H20 A:LHT304 4.2 37.8 1.0 CD2 A:HIS86 4.2 13.7 1.0 C17 A:LHT304 4.2 30.0 1.0 HE2 A:PHE124 4.2 34.0 1.0 CD2 A:HIS89 4.3 16.2 1.0 N3 A:LHT304 4.3 35.1 1.0 OD1 A:ASP88 4.3 15.7 1.0 HG23 A:THR161 4.4 18.8 1.0 C16 A:LHT304 4.4 37.0 1.0 NE2 A:HIS89 4.4 17.8 1.0 HG A:SER185 4.5 24.5 1.0 H17 A:LHT304 4.5 50.3 1.0 H15 A:LHT304 4.6 38.8 1.0 H19 A:LHT304 4.6 37.8 1.0 C22 A:LHT304 4.7 37.8 1.0 C21 A:LHT304 4.7 50.3 1.0 HB2 A:SER185 4.8 21.4 1.0 HD1 A:HIS84 4.8 19.7 1.0 H A:HIS86 4.9 15.2 1.0 HE2 A:HIS86 4.9 17.8 1.0 CA A:HIS86 4.9 12.3 1.0 HZ A:PHE124 4.9 26.1 1.0 HD1 A:HIS160 4.9 19.9 1.0 HG21 A:THR161 5.0 18.8 1.0 C18 A:LHT304 5.0 35.3 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem


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 the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:20.6 occ:1.00 OD2 A:ASP88 2.1 19.0 1.0 NE2 A:HIS225 2.1 20.9 1.0 NE2 A:HIS89 2.1 17.8 1.0 N3 A:LHT304 2.2 35.1 1.0 O5 A:LHT304 2.3 27.3 1.0 O6 A:LHT304 2.4 33.8 1.0 CG A:ASP88 2.9 18.7 1.0 CE1 A:HIS89 3.0 17.1 1.0 C16 A:LHT304 3.0 37.0 1.0 CE1 A:HIS225 3.0 20.3 1.0 OD1 A:ASP88 3.1 15.7 1.0 CD2 A:HIS89 3.1 16.2 1.0 CD2 A:HIS225 3.1 21.3 1.0 HE1 A:HIS89 3.1 20.5 1.0 HE1 A:HIS225 3.1 24.4 1.0 C17 A:LHT304 3.1 30.0 1.0 HD2 A:HIS225 3.3 25.5 1.0 HD2 A:HIS89 3.3 19.4 1.0 C20 A:LHT304 3.4 45.0 1.0 C18 A:LHT304 3.4 35.3 1.0 H17 A:LHT304 3.5 50.3 1.0 H2 A:LHT304 3.6 35.3 1.0 C19 A:LHT304 3.8 38.7 1.0 HE1 A:HIS84 3.8 20.9 1.0 ZN A:ZN301 3.9 16.3 1.0 HG A:SER185 4.0 24.5 1.0 ND1 A:HIS89 4.1 14.5 1.0 C21 A:LHT304 4.1 50.3 1.0 ND1 A:HIS225 4.1 19.8 1.0 CG A:HIS89 4.2 15.3 1.0 CG A:HIS225 4.2 19.2 1.0 CB A:ASP88 4.2 16.3 1.0 HB2 A:ASP88 4.3 19.5 1.0 O4 A:LHT304 4.4 29.4 1.0 C3 A:LHT304 4.4 44.9 1.0 CE1 A:HIS84 4.4 17.4 1.0 NE2 A:HIS84 4.4 15.0 1.0 O7 A:LHT304 4.5 26.4 1.0 C2 A:LHT304 4.6 41.2 1.0 HH2 A:TRP17 4.6 28.1 1.0 HZ3 A:TRP17 4.6 24.9 1.0 H15 A:LHT304 4.7 38.8 1.0 HB3 A:ASP88 4.8 19.5 1.0 OG A:SER185 4.8 20.4 1.0 HD21 A:LEU38 4.8 22.1 1.0 HD1 A:HIS89 4.8 17.4 1.0 HB2 A:PRO224 4.9 23.1 1.0 H9 A:LHT304 4.9 41.2 1.0 HD1 A:HIS225 4.9 23.7 1.0 HB2 A:HIS86 4.9 15.4 1.0 CH2 A:TRP17 5.0 23.4 1.0 H7 A:LHT304 5.0 59.3 1.0 HD22 A:LEU38 5.0 22.1 1.0 CZ3 A:TRP17 5.0 20.7 1.0 O8 A:LHT304 5.0 53.3 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the B3 Metallo-Beta-Lactamase L1 with Hydrolysed Ertapenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:67.9 occ:0.50 NE2 A:HIS29 2.2 72.9 1.0 O A:HOH662 2.3 55.2 0.5 HE1 A:HIS29 2.7 69.8 1.0 CE1 A:HIS29 2.7 58.1 1.0 HB3 A:ASP28 3.2 31.7 1.0 CD2 A:HIS29 3.3 57.6 1.0 HD2 A:HIS29 3.7 69.2 1.0 ND1 A:HIS29 3.9 49.3 1.0 O A:HOH637 4.0 56.8 1.0 CB A:ASP28 4.1 26.4 1.0 CG A:HIS29 4.2 37.1 1.0 HB2 A:ASP28 4.3 31.7 1.0 HD1 A:HIS29 4.5 59.2 1.0 O A:HOH591 4.6 45.1 1.0 OD2 A:ASP28 4.6 34.9 1.0 CG A:ASP28 4.7 39.4 1.0 O A:ASP28 4.8 28.1 1.0 HG1 A:THR172 4.8 42.5 1.0 OG1 A:THR172 5.0 35.5 1.0 C A:ASP28 5.0 26.0 1.0

P.Hinchliffe, J.Spencer. Crystal Structure of B3 Metallo-Beta-Lactamase L1 with Bound, Hydrolysed Ertapenem To Be Published.