Zinc in PDB 5w8w: Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement

All present enzymatic activity of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement:
3.5.2.6;

The structure of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement, PDB code: 5w8w was solved by J.M.Gonzalez, I.G.Shabalin, J.E.Raczynska, M.Jaskolski, W.Minor, A.Wlodawer, M.M.Gonzalez, A.J.Vila, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.40 / 2.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.603, 60.419, 69.513, 90.00, 93.28, 90.00
R / Rfree (%)	15.3 / 21.9

The binding sites of Zinc atom in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement (pdb code 5w8w). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement, PDB code: 5w8w:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:33.1 occ:1.00 NE2 A:HIS179 2.0 30.8 1.0 NE2 A:HIS116 2.1 26.6 1.0 ND1 A:HIS118 2.1 30.0 1.0 O A:HOH452 2.2 29.5 1.0 CD2 A:HIS179 3.0 29.7 1.0 CE1 A:HIS179 3.0 31.6 1.0 CD2 A:HIS116 3.1 25.9 1.0 CE1 A:HIS118 3.1 29.3 1.0 CE1 A:HIS116 3.1 25.9 1.0 CG A:HIS118 3.1 28.7 1.0 CB A:HIS118 3.4 28.3 1.0 ZN A:ZN302 3.6 55.8 1.0 OD1 A:ASP120 4.0 36.9 1.0 CB A:CYS198 4.1 32.4 1.0 ND1 A:HIS179 4.1 30.3 1.0 CG A:HIS179 4.2 29.1 1.0 ND1 A:HIS116 4.2 25.1 1.0 CG A:HIS116 4.2 24.6 1.0 NE2 A:HIS118 4.2 28.7 1.0 CD2 A:HIS118 4.2 28.2 1.0 SG A:CYS198 4.3 37.6 1.0 CG2 A:THR180 4.5 23.5 1.0 OD2 A:ASP120 4.7 43.3 1.0 CG A:ASP120 4.8 39.8 1.0 CA A:HIS118 4.9 29.3 1.0

Zinc binding site 2 out of 2 in the Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Bacillus Cereus Zn-Dependent Metallo-Beta-Lactamase at pH 7 - New Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:55.8 occ:1.00 NE2 A:HIS240 2.1 42.5 1.0 OD2 A:ASP120 2.2 43.3 1.0 O A:HOH452 2.2 29.5 1.0 SG A:CYS198 2.3 37.6 1.0 CE1 A:HIS240 3.1 42.3 1.0 CD2 A:HIS240 3.1 40.3 1.0 CG A:ASP120 3.1 39.8 1.0 CB A:CYS198 3.3 32.4 1.0 OD1 A:ASP120 3.4 36.9 1.0 ZN A:ZN301 3.6 33.1 1.0 NH2 A:ARG121 4.1 33.3 1.0 NE A:ARG121 4.1 33.3 1.0 ND1 A:HIS240 4.2 42.0 1.0 CG A:HIS240 4.3 39.5 1.0 CE1 A:HIS116 4.4 25.9 1.0 NE2 A:HIS179 4.4 30.8 1.0 NE2 A:HIS116 4.4 26.6 1.0 CB A:ASP120 4.5 38.6 1.0 CZ A:ARG121 4.5 33.3 1.0 CA A:CYS198 4.6 31.0 1.0 UNK A:UNX303 4.6 51.0 1.0 CE1 A:HIS179 4.7 31.6 1.0

J.E.Raczynska, I.G.Shabalin, W.Minor, A.Wlodawer, M.Jaskolski. A Close Look Onto Structural Models and Primary Ligands of Metallo-Beta-Lactamases. Drug Resist. Updat. V. 40 1 2018.
ISSN: ESSN 1532-2084
PubMed: 30466711
DOI: 10.1016/J.DRUP.2018.08.001