Zinc in PDB 7ayj: Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor.

The structure of Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor., PDB code: 7ayj was solved by A.J.M.Farley, I.Ermolovich, K.Calvopina, P.Rabe, J.Brem, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.19 / 1.21
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.533, 67.43, 40.267, 90, 93.51, 90
R / Rfree (%)	17 / 19.5

The structure of Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor. also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Zinc atom in the Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor. (pdb code 7ayj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor., PDB code: 7ayj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:16.5 occ:0.75 H7 A:S9N303 1.6 19.9 0.8 NE2 A:HIS179 2.1 17.2 1.0 ND1 A:HIS116 2.1 17.6 1.0 N1 A:S9N303 2.2 16.6 0.8 NE2 A:HIS114 2.2 17.4 1.0 H8 A:S9N303 2.8 19.9 0.8 O2 A:S9N303 2.8 19.1 0.8 S A:S9N303 2.9 18.4 0.8 HB2 A:HIS116 2.9 16.0 1.0 CD2 A:HIS179 3.0 16.2 1.0 CE1 A:HIS116 3.0 18.2 1.0 CE1 A:HIS179 3.0 16.9 1.0 CG A:HIS116 3.1 15.2 1.0 CE1 A:HIS114 3.1 12.8 1.0 OD1 A:CYS198 3.1 21.7 0.2 CD2 A:HIS114 3.1 15.0 1.0 HD2 A:HIS179 3.2 19.4 1.0 HE1 A:HIS116 3.2 21.9 1.0 HE1 A:HIS179 3.2 20.2 1.0 HD2 A:HIS114 3.3 18.0 1.0 HE1 A:HIS114 3.3 15.4 1.0 CB A:HIS116 3.4 13.3 1.0 ZN A:ZN302 3.6 16.5 0.8 O3 A:S9N303 3.6 21.2 0.8 HB3 A:HIS116 3.7 16.0 1.0 HB3 A:CYS198 3.8 21.4 0.2 HB2 A:CYS198 3.9 21.9 0.8 O1 A:S9N303 3.9 16.0 0.8 OD1 A:ASP118 4.0 19.4 1.0 HB3 A:CYS198 4.1 21.9 0.8 ND1 A:HIS179 4.1 16.9 1.0 CG A:HIS179 4.1 15.4 1.0 NE2 A:HIS116 4.1 18.1 1.0 HB2 A:CYS198 4.1 21.4 0.2 H A:S9N303 4.1 19.2 0.8 CD2 A:HIS116 4.2 18.7 1.0 ND1 A:HIS114 4.2 14.3 1.0 SG A:CYS198 4.2 16.7 0.8 CB A:CYS198 4.2 18.2 0.8 CG A:HIS114 4.2 13.1 1.0 CB A:CYS198 4.3 17.8 0.2 SG A:CYS198 4.3 13.2 0.2 HD22 A:ASN210 4.4 41.9 1.0 N A:S9N303 4.4 18.5 0.8 H A:HIS116 4.5 13.5 1.0 C A:S9N303 4.7 17.0 0.8 HD2 A:CYS198 4.7 26.8 0.2 OD2 A:ASP118 4.7 18.7 1.0 HE A:ARG119 4.8 15.4 1.0 CG A:ASP118 4.8 15.4 1.0 HB3 A:SER180 4.8 19.6 1.0 HG2 A:ARG119 4.8 13.2 1.0 CA A:HIS116 4.8 12.2 1.0 HD1 A:HIS179 4.9 20.3 1.0 HE2 A:HIS116 4.9 21.7 1.0 HD1 A:HIS114 5.0 17.2 1.0 HG3 A:ARG119 5.0 13.2 1.0 C1 A:S9N303 5.0 17.8 0.8

Zinc binding site 2 out of 2 in the Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo Beta-Lactamse Vim-1 with A Sulfamoyl Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:16.5 occ:0.75 HD2 A:CYS198 1.6 26.8 0.2 OD1 A:CYS198 1.8 21.7 0.2 H8 A:S9N303 1.9 19.9 0.8 N1 A:S9N303 1.9 16.6 0.8 H7 A:S9N303 2.0 19.9 0.8 OD2 A:CYS198 2.0 22.4 0.2 O1 A:S9N303 2.0 16.0 0.8 NE2 A:HIS240 2.1 13.3 0.8 SG A:CYS198 2.2 16.7 0.8 SG A:CYS198 2.5 13.2 0.2 OD2 A:ASP118 2.6 18.7 1.0 H A:S9N303 2.7 19.2 0.8 C A:S9N303 3.0 17.0 0.8 CD2 A:HIS240 3.0 13.0 0.8 S A:S9N303 3.1 18.4 0.8 N A:S9N303 3.1 18.5 0.8 HB2 A:CYS198 3.1 21.4 0.2 HD2 A:HIS240 3.1 15.5 0.8 HB3 A:CYS198 3.2 21.9 0.8 CE1 A:HIS240 3.2 14.4 0.8 C1 A:S9N303 3.2 17.8 0.8 HH21 A:ARG119 3.2 17.9 1.0 CB A:CYS198 3.3 18.2 0.8 CB A:CYS198 3.3 17.8 0.2 HE1 A:HIS240 3.4 17.2 0.8 CG A:ASP118 3.5 15.4 1.0 ZN A:ZN301 3.6 16.5 0.8 HE A:ARG119 3.7 15.4 1.0 OD1 A:ASP118 3.8 19.4 1.0 HE1 A:HIS114 3.8 15.4 1.0 HB2 A:CYS198 3.8 21.9 0.8 O2 A:S9N303 3.9 19.1 0.8 HB3 A:CYS198 3.9 21.4 0.2 HD2 A:HIS240 3.9 21.0 0.2 NH2 A:ARG119 3.9 15.0 1.0 O3 A:S9N303 4.1 21.2 0.8 C10 A:S9N303 4.1 24.7 0.8 O A:HOH549 4.2 19.6 1.0 O A:S9N303 4.2 18.2 0.8 HE1 A:HIS179 4.2 20.2 1.0 CG A:HIS240 4.2 14.5 0.8 ND1 A:HIS240 4.2 14.3 0.8 NE2 A:HIS179 4.2 17.2 1.0 C2 A:S9N303 4.3 19.4 0.8 CE1 A:HIS179 4.3 16.9 1.0 HH22 A:ARG119 4.4 17.9 1.0 NE A:ARG119 4.4 12.9 1.0 CE1 A:HIS114 4.4 12.8 1.0 HA A:CYS198 4.4 18.0 0.8 H4 A:S9N303 4.5 32.1 0.8 NE2 A:HIS114 4.5 17.4 1.0 CA A:CYS198 4.5 15.1 0.8 CA A:CYS198 4.6 15.2 0.2 CZ A:ARG119 4.6 12.9 1.0 HA3 A:GLY239 4.6 16.8 1.0 H6 A:S9N303 4.7 29.7 0.8 C9 A:S9N303 4.7 21.8 0.8 CD2 A:HIS240 4.8 17.5 0.2 HB3 A:HIS240 4.8 24.2 0.2 CB A:ASP118 4.9 14.3 1.0

A.J.M.Farley, A.J.M.Farley, I.Ermolovich, K.Calvopina, P.Rabe, J.Brem, C.J.Schofield. N/A N/A.