Zinc in PDB 4c1g: Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with D-Captopril

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

The structure of Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with D-Captopril, PDB code: 4c1g 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)	52.543 / 1.71
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.220, 54.570, 194.590, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 17.58

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with D-Captopril (pdb code 4c1g). 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 D-Captopril, PDB code: 4c1g:
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 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 Imp-1 with D-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:19.0 occ:1.00 ND1 A:HIS97 2.0 20.0 1.0 NE2 A:HIS157 2.0 18.6 1.0 NE2 A:HIS95 2.1 18.5 1.0 S A:MCO305 2.4 40.2 1.0 CD2 A:HIS95 2.9 16.3 1.0 CE1 A:HIS97 2.9 19.5 1.0 CD2 A:HIS157 2.9 19.4 1.0 CG A:HIS97 3.0 17.4 1.0 CE1 A:HIS157 3.0 20.8 1.0 CE1 A:HIS95 3.2 17.9 1.0 CB A:HIS97 3.4 16.8 1.0 C1 A:MCO305 3.4 36.0 1.0 ZN A:ZN301 3.7 18.6 1.0 CB A:CYS176 4.0 19.6 1.0 NE2 A:HIS97 4.1 19.5 1.0 SG A:CYS176 4.1 19.3 1.0 CD2 A:HIS97 4.1 17.9 1.0 CG A:HIS157 4.1 15.5 1.0 ND1 A:HIS157 4.1 19.8 1.0 O A:HOH2168 4.1 44.5 1.0 CG A:HIS95 4.2 14.7 1.0 OD1 A:ASP99 4.2 19.2 1.0 ND1 A:HIS95 4.3 17.5 1.0 CG2 A:THR158 4.5 17.9 1.0 O1 A:MCO305 4.7 32.3 1.0 C2 A:MCO305 4.7 34.0 1.0 CA A:HIS97 4.8 15.3 1.0 O A:HOH2198 4.9 56.1 1.0 C4 A:MCO305 5.0 32.4 1.0 OD2 A:ASP99 5.0 19.1 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 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 Imp-1 with D-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:18.6 occ:1.00 NE2 A:HIS215 2.0 17.8 1.0 OD2 A:ASP99 2.3 19.1 1.0 SG A:CYS176 2.3 19.3 1.0 S A:MCO305 2.3 40.2 1.0 CE1 A:HIS215 3.0 17.1 1.0 CD2 A:HIS215 3.0 20.5 1.0 CG A:ASP99 3.1 18.3 1.0 OD1 A:ASP99 3.3 19.2 1.0 C1 A:MCO305 3.4 36.0 1.0 CB A:CYS176 3.5 19.6 1.0 ZN A:ZN300 3.7 19.0 1.0 C2 A:MCO305 4.0 34.0 1.0 ND1 A:HIS215 4.1 19.6 1.0 CE1 A:HIS95 4.1 17.9 1.0 NE2 A:HIS95 4.2 18.5 1.0 CG A:HIS215 4.2 15.6 1.0 CB A:SER214 4.3 17.2 1.0 CE A:LYS51 4.5 18.8 1.0 CA A:CYS176 4.5 19.7 1.0 CD A:LYS51 4.5 15.1 1.0 CB A:ASP99 4.5 17.6 1.0 C4 A:MCO305 4.6 32.4 1.0 NE2 A:HIS157 4.6 18.6 1.0 OG A:SER214 4.6 19.0 1.0 C5 A:MCO305 4.9 31.4 1.0 N A:MCO305 5.0 31.4 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with D-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 D-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn300 b:63.5 occ:1.00 OD2 B:ASP99 2.0 66.2 1.0 NE2 B:HIS215 2.1 61.4 1.0 SG B:CYS176 2.1 62.1 1.0 O B:HOH2005 2.2 54.1 1.0 CE1 B:HIS215 3.0 59.7 1.0 CG B:ASP99 3.1 66.9 1.0 CD2 B:HIS215 3.1 59.0 1.0 OD1 B:ASP99 3.4 66.0 1.0 CB B:CYS176 3.5 58.8 1.0 ZN B:ZN301 3.6 61.9 1.0 NE2 B:HIS95 4.1 63.7 1.0 CE1 B:HIS95 4.1 66.0 1.0 ND1 B:HIS215 4.1 59.0 1.0 CG B:HIS215 4.2 57.7 1.0 CE B:LYS51 4.3 61.2 1.0 CB B:ASP99 4.4 67.6 1.0 CB B:SER214 4.4 59.7 1.0 CA B:CYS176 4.5 61.0 1.0 CD B:LYS51 4.5 61.6 1.0 NE2 B:HIS157 4.7 61.5 1.0 OG B:SER214 4.8 60.1 1.0 CE1 B:HIS157 4.9 64.7 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of the Metallo-Beta-Lactamase Imp-1 with D-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 D-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:61.9 occ:1.00 NE2 B:HIS157 2.1 61.5 1.0 ND1 B:HIS97 2.1 62.7 1.0 NE2 B:HIS95 2.1 63.7 1.0 O B:HOH2005 2.2 54.1 1.0 CE1 B:HIS157 2.5 64.7 1.0 CD2 B:HIS95 2.9 65.9 1.0 CE1 B:HIS97 2.9 62.7 1.0 CG B:HIS97 3.0 64.7 1.0 CE1 B:HIS95 3.3 66.0 1.0 CD2 B:HIS157 3.4 62.0 1.0 CB B:HIS97 3.4 66.1 1.0 ZN B:ZN300 3.6 63.5 1.0 ND1 B:HIS157 3.8 64.8 1.0 SG B:CYS176 3.8 62.1 1.0 CB B:CYS176 3.9 58.8 1.0 NE2 B:HIS97 4.0 65.9 1.0 CD2 B:HIS97 4.1 66.1 1.0 OD1 B:ASP99 4.1 66.0 1.0 CG B:HIS95 4.2 67.3 1.0 CG B:HIS157 4.2 63.7 1.0 ND1 B:HIS95 4.3 66.8 1.0 CG2 B:THR158 4.4 67.6 1.0 OD2 B:ASP99 4.6 66.2 1.0 CG B:ASP99 4.8 66.9 1.0 CA B:HIS97 4.8 65.5 1.0

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