Zinc in PDB 4c09: Crystal Structure of the Metallo-Beta-Lactamase Bcii

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Bcii:
3.5.2.6;

The structure of Crystal Structure of the Metallo-Beta-Lactamase Bcii, PDB code: 4c09 was solved by D.Zollman, J.Brem, M.A.Mcdonough, S.S.Vanberkel, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.681 / 1.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.300, 61.970, 69.460, 90.00, 93.04, 90.00
R / Rfree (%)	11.86 / 13.93

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase Bcii (pdb code 4c09). 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 the Metallo-Beta-Lactamase Bcii, PDB code: 4c09:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Bcii


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 Metallo-Beta-Lactamase Bcii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn350 b:13.4 occ:0.70 O A:HOH2117 2.0 14.3 1.0 NE2 A:HIS240 2.1 16.3 1.0 O A:HOH2192 2.2 18.2 1.0 SG A:CYS198 2.2 14.3 1.0 OD2 A:ASP120 2.3 16.9 1.0 CD2 A:HIS240 3.0 16.1 1.0 CE1 A:HIS240 3.1 15.2 1.0 CB A:CYS198 3.3 12.2 1.0 CG A:ASP120 3.3 14.1 1.0 ZN A:ZN351 3.5 12.9 1.0 OD1 A:ASP120 3.6 18.4 1.0 O A:HOH2122 4.0 31.2 1.0 NE2 A:HIS179 4.1 11.6 1.0 NH2 A:ARG121 4.2 14.6 0.7 ND1 A:HIS240 4.2 15.2 1.0 CG A:HIS240 4.2 16.0 1.0 NE A:ARG121 4.3 11.1 0.7 CE1 A:HIS116 4.3 11.6 1.0 NE2 A:HIS116 4.4 11.9 1.0 NE A:ARG121 4.4 16.7 0.3 CE1 A:HIS179 4.4 11.8 1.0 O A:HOH2206 4.5 16.6 1.0 CA A:CYS198 4.5 11.8 1.0 CB A:ASP120 4.6 14.8 1.0 CZ A:ARG121 4.6 12.3 0.7 NH2 A:ARG121 4.6 18.8 0.3 O A:HOH2045 4.7 42.9 1.0 CZ A:ARG121 4.8 17.1 0.3 CD2 A:HIS179 4.9 10.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Bcii


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 Metallo-Beta-Lactamase Bcii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn351 b:12.9 occ:1.00 O A:HOH2117 2.0 14.3 1.0 ND1 A:HIS118 2.0 16.2 0.3 NE2 A:HIS179 2.0 11.6 1.0 ND1 A:HIS118 2.0 12.1 0.7 NE2 A:HIS116 2.0 11.9 1.0 CE1 A:HIS118 3.0 16.5 0.3 CG A:HIS118 3.0 16.6 0.3 CD2 A:HIS179 3.0 10.5 1.0 CE1 A:HIS118 3.0 11.2 0.7 CG A:HIS118 3.0 12.0 0.7 CE1 A:HIS179 3.0 11.8 1.0 CE1 A:HIS116 3.0 11.6 1.0 CD2 A:HIS116 3.1 10.2 1.0 CB A:HIS118 3.3 16.1 0.3 CB A:HIS118 3.3 12.5 0.7 O A:HOH2122 3.4 31.2 1.0 ZN A:ZN350 3.5 13.4 0.7 O A:HOH2192 3.9 18.2 1.0 OD1 A:ASP120 4.0 18.4 1.0 NE2 A:HIS118 4.0 17.0 0.3 CD2 A:HIS118 4.1 17.1 0.3 NE2 A:HIS118 4.1 12.6 0.7 ND1 A:HIS179 4.1 11.2 1.0 ND1 A:HIS116 4.1 10.5 1.0 CD2 A:HIS118 4.1 13.4 0.7 CG A:HIS179 4.1 10.4 1.0 CB A:CYS198 4.2 12.2 1.0 CG A:HIS116 4.2 9.7 1.0 SG A:CYS198 4.3 14.3 1.0 CG2 A:THR180 4.4 10.6 1.0 OD2 A:ASP120 4.5 16.9 1.0 CG A:ASP120 4.7 14.1 1.0 CA A:HIS118 4.8 14.5 0.3 CA A:HIS118 4.8 13.8 0.7

J.Brem, S.S.Vanberkel, D.Zollman, C.J.Schofield. B1 Mbl Inhibitor Structures. To Be Published.