Zinc in PDB 4c1h: Crystal Structure of the Metallo-Beta-Lactamase Bcii with L-Captopril

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

The structure of Crystal Structure of the Metallo-Beta-Lactamase Bcii with L-Captopril, PDB code: 4c1h 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)	40.074 / 1.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.009, 61.336, 69.580, 90.00, 93.03, 90.00
R / Rfree (%)	13.15 / 13.87

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase Bcii with L-Captopril (pdb code 4c1h). 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 L-Captopril, PDB code: 4c1h:
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 L-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 L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn350 b:11.1 occ:0.70 OD2 A:ASP120 2.0 13.9 1.0 NE2 A:HIS240 2.1 13.5 1.0 SG A:CYS198 2.2 10.1 1.0 S A:X8Z305 2.3 11.7 0.7 O A:HOH2111 2.8 26.4 0.3 CG A:ASP120 2.9 13.8 1.0 CE1 A:HIS240 3.0 14.1 1.0 CD2 A:HIS240 3.1 14.2 1.0 OD1 A:ASP120 3.3 15.5 1.0 CB A:CYS198 3.3 10.7 1.0 C1 A:X8Z305 3.4 13.2 0.7 ZN A:ZN351 3.8 12.0 1.0 NE A:ARG121 3.8 13.6 0.3 NE A:ARG121 4.0 10.4 0.7 C2 A:X8Z305 4.0 15.1 0.7 NH2 A:ARG121 4.0 12.1 0.7 NH2 A:ARG121 4.0 13.6 0.3 ND1 A:HIS240 4.1 14.5 1.0 CG A:HIS240 4.2 14.6 1.0 CB A:ASP120 4.2 13.7 1.0 CE1 A:HIS116 4.2 10.9 1.0 CZ A:ARG121 4.2 13.6 0.3 CZ A:ARG121 4.3 10.9 0.7 NE2 A:HIS116 4.4 11.1 1.0 CA A:CYS198 4.6 10.3 1.0 NE2 A:HIS179 4.6 11.6 1.0 C4 A:X8Z305 4.7 16.8 0.7 CD A:ARG121 4.7 13.1 0.3 C5 A:X8Z305 4.8 19.0 0.7 CD A:ARG121 4.8 10.2 0.7 CG A:ARG121 4.8 13.0 0.3 O A:GLY239 5.0 14.3 1.0 O A:HOH2201 5.0 15.6 1.0 N A:X8Z305 5.0 18.2 0.7

Zinc binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Bcii with L-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 L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn351 b:12.0 occ:1.00 O A:HOH2111 1.9 26.4 0.3 NE2 A:HIS116 2.0 11.1 1.0 NE2 A:HIS179 2.0 11.6 1.0 ND1 A:HIS118 2.0 12.9 0.5 ND1 A:HIS118 2.0 12.2 0.5 S A:X8Z305 2.3 11.7 0.7 CE1 A:HIS116 3.0 10.9 1.0 CD2 A:HIS116 3.0 10.2 1.0 CE1 A:HIS179 3.0 12.3 1.0 CG A:HIS118 3.0 12.6 0.5 CG A:HIS118 3.0 12.9 0.5 CE1 A:HIS118 3.0 12.8 0.5 CE1 A:HIS118 3.0 11.9 0.5 CD2 A:HIS179 3.1 11.0 1.0 C1 A:X8Z305 3.2 13.2 0.7 CB A:HIS118 3.3 12.8 0.5 CB A:HIS118 3.3 12.7 0.5 ZN A:ZN350 3.8 11.1 0.7 CB A:CYS198 4.1 10.7 1.0 ND1 A:HIS116 4.1 10.5 1.0 ND1 A:HIS179 4.1 11.9 1.0 OD1 A:ASP120 4.1 15.5 1.0 CG A:HIS116 4.1 9.8 1.0 NE2 A:HIS118 4.1 13.2 0.5 NE2 A:HIS118 4.1 12.5 0.5 CD2 A:HIS118 4.2 13.0 0.5 CD2 A:HIS118 4.2 12.5 0.5 CG A:HIS179 4.2 11.0 1.0 CG2 A:THR180 4.3 9.9 1.0 SG A:CYS198 4.3 10.1 1.0 C2 A:X8Z305 4.6 15.1 0.7 CA A:HIS118 4.8 12.6 0.5 CA A:HIS118 4.8 12.8 0.5 OD2 A:ASP120 4.8 13.9 1.0 O1 A:X8Z305 4.8 17.3 0.7 CG A:ASP120 4.9 13.8 1.0 O A:HOH2186 5.0 20.3 0.7

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