Zinc in PDB 5fqb: Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C

All present enzymatic activity of Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C:
3.5.2.6;

The structure of Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C, PDB code: 5fqb was solved by S.T.Cahill, J.Brem, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.64 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.147, 61.117, 69.390, 90.00, 93.12, 90.00
R / Rfree (%)	14 / 18.1

The binding sites of Zinc atom in the Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C (pdb code 5fqb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C, PDB code: 5fqb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C


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 Bacillus Cereus Metallo-Beta-Lactamase with 2C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn295 b:26.1 occ:0.80 O16 A:OK3297 2.0 25.7 0.7 O26 A:OK3297 2.2 24.0 0.7 SG A:CYS224 2.2 22.0 1.0 NE2 A:HIS266 2.2 26.0 1.0 O A:HOH2059 2.5 20.4 0.3 OD2 A:ASP123 2.6 31.3 1.0 CD2 A:HIS266 3.0 25.3 1.0 C15 A:OK3297 3.0 26.8 0.7 B17 A:OK3297 3.1 22.8 0.7 O18 A:OK3297 3.1 18.9 0.7 C24 A:OK3297 3.1 24.8 0.7 CB A:CYS224 3.2 17.6 1.0 CE1 A:HIS266 3.3 27.8 1.0 C20 A:OK3297 3.4 27.0 0.7 CG A:ASP123 3.7 28.5 1.0 O19 A:OK3297 4.0 17.6 0.7 OD1 A:ASP123 4.0 24.8 1.0 NH2 A:ARG124 4.1 29.3 1.0 O A:HOH2132 4.1 24.8 1.0 C14 A:OK3297 4.1 27.3 0.7 ZN A:ZN296 4.1 20.3 1.0 CG A:HIS266 4.2 25.4 1.0 O25 A:OK3297 4.3 24.0 0.7 C12 A:OK3297 4.3 25.9 0.7 NE2 A:HIS199 4.3 14.0 1.0 CA A:CYS224 4.4 15.7 1.0 ND1 A:HIS266 4.4 28.0 1.0 CE1 A:HIS199 4.4 17.2 1.0 C13 A:OK3297 4.5 26.8 0.7 NE A:ARG124 4.6 24.0 1.0 CZ A:ARG124 4.7 27.9 1.0 C21 A:OK3297 4.8 28.5 0.7 CE1 A:HIS119 4.8 17.3 1.0 CB A:ASP123 4.9 28.9 1.0 NE2 A:HIS119 5.0 16.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Bacillus Cereus Metallo-Beta-Lactamase with 2C


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 Bacillus Cereus Metallo-Beta-Lactamase with 2C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn296 b:20.3 occ:1.00 O18 A:OK3297 1.8 18.9 0.7 ND1 A:HIS121 2.0 20.4 1.0 NE2 A:HIS199 2.0 14.0 1.0 NE2 A:HIS119 2.1 16.7 1.0 O A:HOH2059 2.2 20.4 0.3 O19 A:OK3297 2.7 17.6 0.7 B17 A:OK3297 2.8 22.8 0.7 CG A:HIS121 3.0 21.2 1.0 CE1 A:HIS199 3.0 17.2 1.0 CD2 A:HIS199 3.0 13.8 1.0 CE1 A:HIS121 3.0 23.1 1.0 CE1 A:HIS119 3.0 17.3 1.0 CD2 A:HIS119 3.1 15.8 1.0 CB A:HIS121 3.2 20.5 1.0 O16 A:OK3297 3.6 25.7 0.7 C12 A:OK3297 4.1 25.9 0.7 CD2 A:HIS121 4.1 21.2 1.0 NE2 A:HIS121 4.1 23.2 1.0 ND1 A:HIS199 4.1 16.0 1.0 ZN A:ZN295 4.1 26.1 0.8 ND1 A:HIS119 4.1 14.6 1.0 OD1 A:ASP123 4.1 24.8 1.0 CG2 A:THR200 4.2 14.8 1.0 CG A:HIS199 4.2 15.4 1.0 N11 A:OK3297 4.2 24.8 0.7 CG A:HIS119 4.2 14.5 1.0 CB A:CYS224 4.3 17.6 1.0 SG A:CYS224 4.4 22.0 1.0 CA A:HIS121 4.7 21.8 1.0 OD2 A:ASP123 4.9 31.3 1.0 C15 A:OK3297 4.9 26.8 0.7 O26 A:OK3297 4.9 24.0 0.7 CG A:ASP123 4.9 28.5 1.0

J.Brem, R.Cain, S.Cahill, M.A.Mcdonough, I.J.Clifton, J.C.Jimenez-Castellanos, M.B.Avison, J.Spencer, C.W.Fishwick, C.J.Schofield. Structural Basis of Metallo-Beta-Lactamase, Serine-Beta-Lactamase and Penicillin-Binding Protein Inhibition By Cyclic Boronates. Nat Commun V. 7 12406 2016.
ISSN: ESSN 2041-1723
PubMed: 27499424
DOI: 10.1038/NCOMMS12406