Zinc in PDB 4c1f: Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril:
3.5.2.6;

The structure of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril, PDB code: 4c1f 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)	52.568 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	193.620, 49.910, 54.620, 90.00, 90.00, 90.00
R / Rfree (%)	18.39 / 22.44

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril (pdb code 4c1f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril, PDB code: 4c1f:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 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 Imp-1 with L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:15.2 occ:1.00 NE2 A:HIS157 2.0 16.4 1.0 NE2 A:HIS95 2.2 12.0 1.0 ND1 A:HIS97 2.2 16.0 1.0 S A:X8Z300 2.3 16.9 1.0 CD2 A:HIS157 3.0 13.4 1.0 CD2 A:HIS95 3.0 10.3 1.0 CE1 A:HIS157 3.0 12.5 1.0 CG A:HIS97 3.2 16.2 1.0 CE1 A:HIS97 3.2 18.4 1.0 C1 A:X8Z300 3.3 26.2 1.0 CE1 A:HIS95 3.3 16.4 1.0 CB A:HIS97 3.4 16.1 1.0 ZN A:ZN502 3.6 17.8 1.0 CB A:CYS176 4.1 14.8 1.0 ND1 A:HIS157 4.1 16.1 1.0 CG A:HIS157 4.2 14.2 1.0 OD1 A:ASP99 4.2 15.6 1.0 SG A:CYS176 4.2 15.5 1.0 CG A:HIS95 4.2 9.8 1.0 NE2 A:HIS97 4.3 19.6 1.0 ND1 A:HIS95 4.3 12.7 1.0 CD2 A:HIS97 4.3 18.1 1.0 C2 A:X8Z300 4.6 30.4 1.0 CG2 A:THR158 4.7 17.0 1.0 OD2 A:ASP99 4.7 16.0 1.0 CA A:HIS97 4.9 13.9 1.0 CG A:ASP99 4.9 14.1 1.0 O2 A:X8Z300 4.9 49.0 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 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 Imp-1 with L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:17.8 occ:1.00 NE2 A:HIS215 2.0 11.8 1.0 OD2 A:ASP99 2.0 16.0 1.0 S A:X8Z300 2.2 16.9 1.0 SG A:CYS176 2.4 15.5 1.0 CE1 A:HIS215 2.8 10.8 1.0 CG A:ASP99 3.0 14.1 1.0 CD2 A:HIS215 3.1 11.9 1.0 C1 A:X8Z300 3.3 26.2 1.0 OD1 A:ASP99 3.3 15.6 1.0 CB A:CYS176 3.4 14.8 1.0 C2 A:X8Z300 3.6 30.4 1.0 ZN A:ZN501 3.6 15.2 1.0 O3 A:X8Z300 4.0 46.1 1.0 ND1 A:HIS215 4.0 12.0 1.0 CE1 A:HIS95 4.1 16.4 1.0 CG A:HIS215 4.2 11.9 1.0 NE2 A:HIS95 4.2 12.0 1.0 C9 A:X8Z300 4.3 46.4 1.0 CB A:ASP99 4.4 14.6 1.0 CB A:SER214 4.4 15.9 1.0 C3 A:X8Z300 4.4 29.2 1.0 C8 A:X8Z300 4.5 42.3 1.0 CD A:LYS51 4.5 14.4 1.0 CE A:LYS51 4.6 12.2 1.0 CA A:CYS176 4.6 15.4 1.0 NE2 A:HIS157 4.6 16.4 1.0 OG A:SER214 4.6 18.1 1.0 C4 A:X8Z300 4.8 36.1 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:56.7 occ:1.00 OD2 B:ASP99 1.8 54.2 1.0 SG B:CYS176 2.0 56.3 1.0 NE2 B:HIS215 2.1 52.4 1.0 O B:HOH2004 2.8 42.1 1.0 CG B:ASP99 2.9 49.7 1.0 CE1 B:HIS215 3.0 52.5 1.0 CD2 B:HIS215 3.1 49.6 1.0 OD1 B:ASP99 3.4 46.9 1.0 ZN B:ZN502 3.6 57.2 1.0 CB B:CYS176 3.7 54.9 1.0 ND1 B:HIS215 4.1 52.3 1.0 NE2 B:HIS95 4.2 61.5 1.0 CB B:ASP99 4.2 51.9 1.0 CG B:HIS215 4.2 49.5 1.0 CE1 B:HIS95 4.2 64.3 1.0 CB B:SER214 4.3 52.9 1.0 CD B:LYS51 4.5 54.7 1.0 NZ B:LYS51 4.5 58.4 1.0 OG B:SER214 4.7 53.9 1.0 CA B:CYS176 4.7 55.8 1.0 NE2 B:HIS157 4.8 53.3 1.0 CE B:LYS51 5.0 55.5 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:57.2 occ:1.00 NE2 B:HIS157 1.9 53.3 1.0 ND1 B:HIS97 2.0 61.7 1.0 NE2 B:HIS95 2.1 61.5 1.0 CE1 B:HIS157 2.6 52.9 1.0 O B:HOH2004 2.6 42.1 1.0 CD2 B:HIS95 2.9 65.0 1.0 CE1 B:HIS97 2.9 64.4 1.0 CG B:HIS97 2.9 64.9 1.0 CD2 B:HIS157 3.1 51.3 1.0 CE1 B:HIS95 3.2 64.3 1.0 CB B:HIS97 3.4 66.5 1.0 SG B:CYS176 3.5 56.3 1.0 ZN B:ZN501 3.6 56.7 1.0 ND1 B:HIS157 3.8 52.6 1.0 CB B:CYS176 3.9 54.9 1.0 NE2 B:HIS97 4.0 65.8 1.0 CD2 B:HIS97 4.1 66.2 1.0 CG B:HIS157 4.1 52.4 1.0 CG B:HIS95 4.1 67.7 1.0 ND1 B:HIS95 4.3 66.8 1.0 OD1 B:ASP99 4.3 46.9 1.0 OD2 B:ASP99 4.4 54.2 1.0 CG2 B:THR158 4.6 55.2 1.0 CG B:ASP99 4.8 49.7 1.0 CA B:HIS97 4.8 67.0 1.0

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