Zinc in PDB 4c1c: Crystal Structure of the Metallo-Beta-Lactamase Bcii with D-Captopril

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

The structure of Crystal Structure of the Metallo-Beta-Lactamase Bcii with D-Captopril, PDB code: 4c1c 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)	40.195 / 1.18
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.160, 61.530, 69.520, 90.00, 92.98, 90.00
R / Rfree (%)	12 / 13.55

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase Bcii with D-Captopril (pdb code 4c1c). 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 with D-Captopril, PDB code: 4c1c:
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 with D-Captopril


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 with D-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1262 b:11.9 occ:0.70 OD2 A:ASP120 1.9 17.3 1.0 NE2 A:HIS240 2.1 16.0 1.0 SG A:CYS198 2.3 13.2 1.0 S A:MCO1261 2.3 40.2 0.7 O A:HOH2091 2.4 21.5 0.3 CG A:ASP120 2.9 14.6 1.0 CE1 A:HIS240 3.0 15.9 1.0 CD2 A:HIS240 3.1 16.3 1.0 OD1 A:ASP120 3.3 17.6 1.0 CB A:CYS198 3.4 12.0 1.0 C1 A:MCO1261 3.4 36.0 0.7 ZN A:ZN1263 3.8 12.6 1.0 NE A:ARG121 3.9 14.4 1.0 C2 A:MCO1261 4.0 34.0 0.7 NH2 A:ARG121 4.0 17.9 1.0 ND1 A:HIS240 4.1 15.7 1.0 CG A:HIS240 4.2 16.0 1.0 CB A:ASP120 4.2 15.4 1.0 CE1 A:HIS116 4.3 11.4 1.0 O2 A:MCO1261 4.3 24.4 0.7 CZ A:ARG121 4.3 14.6 1.0 NE2 A:HIS116 4.4 12.0 1.0 C4 A:MCO1261 4.5 32.4 0.7 C5 A:MCO1261 4.7 31.4 0.7 NE2 A:HIS179 4.7 11.7 1.0 CA A:CYS198 4.7 11.1 1.0 N A:MCO1261 4.8 31.4 0.7 CD A:ARG121 4.9 13.7 1.0 O A:GLY239 5.0 15.7 1.0

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


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 with D-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1263 b:12.6 occ:1.00 ND1 A:HIS118 2.0 13.2 1.0 NE2 A:HIS179 2.0 11.7 1.0 NE2 A:HIS116 2.0 12.0 1.0 O A:HOH2091 2.2 21.5 0.3 S A:MCO1261 2.3 40.2 0.7 CE1 A:HIS179 3.0 11.7 1.0 CE1 A:HIS116 3.0 11.4 1.0 CE1 A:HIS118 3.0 12.6 1.0 CG A:HIS118 3.0 12.9 1.0 CD2 A:HIS116 3.0 10.9 1.0 CD2 A:HIS179 3.0 10.7 1.0 C1 A:MCO1261 3.3 36.0 0.7 CB A:HIS118 3.3 13.9 1.0 ZN A:ZN1262 3.8 11.9 0.7 ND1 A:HIS116 4.1 10.7 1.0 CB A:CYS198 4.1 12.0 1.0 NE2 A:HIS118 4.1 13.8 1.0 ND1 A:HIS179 4.1 11.7 1.0 OD1 A:ASP120 4.1 17.6 1.0 CD2 A:HIS118 4.1 13.2 1.0 CG A:HIS116 4.1 10.1 1.0 CG A:HIS179 4.2 10.5 1.0 CG2 A:THR180 4.3 10.4 1.0 SG A:CYS198 4.4 13.2 1.0 O1 A:MCO1261 4.6 32.3 0.7 C2 A:MCO1261 4.6 34.0 0.7 CA A:HIS118 4.8 14.3 1.0 OD2 A:ASP120 4.8 17.3 1.0 C4 A:MCO1261 4.9 32.4 0.7 CG A:ASP120 4.9 14.6 1.0

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