Sodium in PDB 4c1d: Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril:
3.5.2.6;

The structure of Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril, PDB code: 4c1d 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)	39.701 / 1.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.246, 79.402, 67.774, 90.00, 130.30, 90.00
R / Rfree (%)	14.27 / 17.22

The structure of Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril also contains other interesting chemical elements:

Zinc

(Zn)

6 atoms

The binding sites of Sodium atom in the Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril (pdb code 4c1d). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril, PDB code: 4c1d:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Na300 b:29.1 occ:0.80 O A:HOH2140 2.1 35.0 1.0 OE1 A:GLU171 2.2 26.8 1.0 NE2 A:HIS229 2.2 28.2 1.0 O A:HOH2139 2.3 32.4 1.0 OE2 A:GLU171 2.6 30.4 1.0 CD A:GLU171 2.7 26.3 1.0 CD2 A:HIS229 2.9 26.2 1.0 CE1 A:HIS229 3.3 27.6 1.0 OH A:TYR230 4.1 20.6 1.0 CG A:HIS229 4.1 21.3 1.0 CE1 A:TYR230 4.1 16.9 1.0 CG A:GLU171 4.2 22.0 1.0 ND1 A:HIS229 4.3 25.7 1.0 O A:HOH2193 4.3 26.0 1.0 CZ A:TYR230 4.4 18.4 1.0 CB A:ALA164 4.6 20.1 1.0 O A:HIS229 4.9 16.4 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the Metallo-Beta-Lactamase Vim-2 with L-Captopril within 5.0Å range: probe atom residue distance (Å) B Occ B:Na300 b:28.1 occ:0.80 OE1 B:GLU171 2.0 22.4 1.0 O B:HOH2128 2.1 31.5 1.0 NE2 B:HIS229 2.1 25.9 1.0 O B:HOH2129 2.3 32.3 1.0 CD B:GLU171 2.7 21.1 1.0 OE2 B:GLU171 2.8 26.0 1.0 CD2 B:HIS229 2.9 22.9 1.0 O B:HOH2205 2.9 36.9 1.0 CE1 B:HIS229 3.2 24.3 1.0 OH B:TYR230 4.0 16.6 1.0 CE1 B:TYR230 4.1 15.6 1.0 CG B:HIS229 4.1 19.0 1.0 O B:HOH2178 4.2 24.6 1.0 ND1 B:HIS229 4.2 23.4 1.0 CG B:GLU171 4.2 17.0 1.0 CZ B:TYR230 4.3 15.6 1.0 CB B:ALA164 4.4 16.4 1.0 O B:HOH2177 4.4 34.6 1.0 O B:HIS229 4.9 16.6 1.0 CD1 B:TYR230 5.0 14.5 1.0

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