Zinc in PDB 6ewe: Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with Dz- 308

All present enzymatic activity of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with Dz- 308:
3.5.2.6;

The structure of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with Dz- 308, PDB code: 6ewe was solved by D.Stepanovs, M.A.Mcdonough, C.J.Schofield, D.Zhang, A.El-Husseiny, J.Brem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.31 / 1.46
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.190, 61.010, 69.540, 90.00, 92.99, 90.00
R / Rfree (%)	13.9 / 16.7

The binding sites of Zinc atom in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with Dz- 308 (pdb code 6ewe). 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 Bcii Metallo-Beta-Lactamase in Complex with Dz- 308, PDB code: 6ewe:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with Dz- 308


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 Bcii Metallo-Beta-Lactamase in Complex with Dz- 308 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:23.5 occ:0.80 SG A:CYS198 2.0 23.5 0.2 NE2 A:HIS240 2.1 22.7 1.0 OD2 A:ASP120 2.2 30.7 1.0 O1 A:C0W304 2.3 27.2 0.8 S A:C0W304 2.3 22.7 0.8 SG A:CYS198 2.4 20.9 0.8 C A:C0W304 3.0 27.2 0.8 CD2 A:HIS240 3.1 22.6 1.0 CE1 A:HIS240 3.1 23.8 1.0 C1 A:C0W304 3.1 28.4 0.8 CG A:ASP120 3.2 29.2 1.0 CB A:CYS198 3.3 20.6 0.8 CB A:CYS198 3.3 22.2 0.2 OD1 A:ASP120 3.5 27.6 1.0 ZN A:ZN302 3.7 20.4 1.0 NH2 A:ARG121 4.1 28.5 1.0 ND1 A:HIS240 4.2 23.2 1.0 NE A:ARG121 4.2 24.0 1.0 CG A:HIS240 4.2 23.5 1.0 O A:C0W304 4.2 28.1 0.8 CE1 A:HIS116 4.3 18.7 1.0 C2 A:C0W304 4.4 32.8 0.8 CB A:ASP120 4.4 28.3 1.0 NE2 A:HIS179 4.5 16.8 1.0 O A:HOH442 4.5 29.8 1.0 NE2 A:HIS116 4.5 18.1 1.0 CZ A:ARG121 4.5 26.7 1.0 CA A:CYS198 4.6 18.9 0.8 CA A:CYS198 4.6 19.9 0.2 CE1 A:HIS179 4.8 19.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with Dz- 308


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 Bcii Metallo-Beta-Lactamase in Complex with Dz- 308 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:20.4 occ:1.00 ND1 A:HIS118 2.0 19.3 1.0 NE2 A:HIS116 2.0 18.1 1.0 NE2 A:HIS179 2.1 16.8 1.0 S A:C0W304 2.3 22.7 0.8 CE1 A:HIS116 2.9 18.7 1.0 CE1 A:HIS118 3.0 21.6 1.0 CD2 A:HIS179 3.0 16.6 1.0 CG A:HIS118 3.0 20.6 1.0 CD2 A:HIS116 3.1 16.7 1.0 CE1 A:HIS179 3.1 19.0 1.0 C1 A:C0W304 3.1 28.4 0.8 CB A:HIS118 3.4 20.1 1.0 C2 A:C0W304 3.7 32.8 0.8 ZN A:ZN301 3.7 23.5 0.8 C A:C0W304 3.9 27.2 0.8 O1 A:C0W304 3.9 27.2 0.8 C3 A:C0W304 4.0 36.1 0.8 OD1 A:ASP120 4.0 27.6 1.0 ND1 A:HIS116 4.1 18.0 1.0 NE2 A:HIS118 4.1 22.6 1.0 CB A:CYS198 4.1 20.6 0.8 CD2 A:HIS118 4.1 22.3 1.0 CG A:HIS116 4.2 16.6 1.0 ND1 A:HIS179 4.2 17.4 1.0 CG A:HIS179 4.2 16.8 1.0 CB A:CYS198 4.2 22.2 0.2 C4 A:C0W304 4.3 37.0 0.8 SG A:CYS198 4.4 20.9 0.8 SG A:CYS198 4.4 23.5 0.2 CG2 A:THR180 4.5 17.8 1.0 C10 A:C0W304 4.6 37.8 0.8 OD2 A:ASP120 4.7 30.7 1.0 CG A:ASP120 4.8 29.2 1.0 CA A:HIS118 4.8 20.4 1.0

D.Zhang, M.S.Markoulides, D.Stepanovs, A.M.Rydzik, A.El-Hussein, C.Bon, J.J.A.G.Kamps, K.D.Umland, P.M.Collins, S.T.Cahill, D.Y.Wang, F.Von Delft, J.Brem, M.A.Mcdonough, C.J.Schofield. Structure Activity Relationship Studies on Rhodanines and Derived Enethiol Inhibitors of Metallo-Beta-Lactamases. Bioorg. Med. Chem. V. 26 2928 2018.
ISSN: ESSN 1464-3391
PubMed: 29655609
DOI: 10.1016/J.BMC.2018.02.043