Zinc in PDB 6f2n: Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with KDU197

All present enzymatic activity of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with KDU197:
3.5.2.6;

The structure of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with KDU197, PDB code: 6f2n was solved by M.A.Mcdonough, A.El-Hussein, C.J.Schofield, D.Zhang, J.Brem, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.19 / 1.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.169, 61.668, 69.675, 90.00, 93.13, 90.00
R / Rfree (%)	13.4 / 15.1

The binding sites of Zinc atom in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with KDU197 (pdb code 6f2n). 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 KDU197, PDB code: 6f2n:
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 KDU197


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 KDU197 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:13.2 occ:0.75 NE2 A:HIS240 2.0 15.6 1.0 OD2 A:ASP120 2.1 16.0 1.0 O A:CF8304 2.2 14.9 0.8 SG A:CYS198 2.3 13.5 1.0 S A:CF8304 2.3 13.7 0.8 C1 A:CF8304 3.0 15.9 0.8 CD2 A:HIS240 3.0 15.4 1.0 C A:CF8304 3.0 14.6 0.8 CE1 A:HIS240 3.1 15.6 1.0 CG A:ASP120 3.1 14.8 1.0 CB A:CYS198 3.3 11.5 1.0 OD1 A:ASP120 3.5 17.0 1.0 ZN A:ZN302 3.8 12.1 1.0 NH2 A:ARG121 4.1 16.7 1.0 NE A:ARG121 4.2 12.6 1.0 ND1 A:HIS240 4.2 15.7 1.0 CG A:HIS240 4.2 15.1 1.0 O1 A:CF8304 4.2 18.4 0.8 CE1 A:HIS116 4.3 11.2 1.0 C2 A:CF8304 4.4 17.9 0.8 NE2 A:HIS179 4.4 10.3 1.0 CB A:ASP120 4.4 14.6 1.0 NE2 A:HIS116 4.5 9.6 1.0 O A:HOH482 4.5 16.4 1.0 CZ A:ARG121 4.5 13.5 1.0 CA A:CYS198 4.5 10.7 1.0 C11 A:CF8304 4.6 26.3 0.8 CE1 A:HIS179 4.7 11.0 1.0 C9 A:CF8304 4.9 23.8 0.8

Zinc binding site 2 out of 2 in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with KDU197


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 KDU197 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:12.1 occ:1.00 ND1 A:HIS118 2.0 11.8 1.0 NE2 A:HIS179 2.0 10.3 1.0 NE2 A:HIS116 2.0 9.6 1.0 S A:CF8304 2.3 13.7 0.8 CE1 A:HIS118 3.0 12.1 1.0 CG A:HIS118 3.0 12.1 1.0 CE1 A:HIS116 3.0 11.2 1.0 CE1 A:HIS179 3.0 11.0 1.0 CD2 A:HIS116 3.0 10.1 1.0 CD2 A:HIS179 3.0 9.5 1.0 C A:CF8304 3.2 14.6 0.8 CB A:HIS118 3.3 14.1 1.0 ZN A:ZN301 3.8 13.2 0.8 C2 A:CF8304 3.9 17.9 0.8 OD1 A:ASP120 4.0 17.0 1.0 O A:CF8304 4.0 14.9 0.8 C1 A:CF8304 4.0 15.9 0.8 NE2 A:HIS118 4.1 13.2 1.0 CD2 A:HIS118 4.1 13.9 1.0 ND1 A:HIS116 4.1 10.1 1.0 C3 A:CF8304 4.1 20.6 0.8 ND1 A:HIS179 4.1 11.6 1.0 CG A:HIS116 4.2 9.1 1.0 CG A:HIS179 4.2 9.9 1.0 CB A:CYS198 4.3 11.5 1.0 CG2 A:THR180 4.3 10.7 1.0 C4 A:CF8304 4.4 21.0 0.8 SG A:CYS198 4.4 13.5 1.0 OD2 A:ASP120 4.7 16.0 1.0 C8 A:CF8304 4.8 22.6 0.8 CA A:HIS118 4.8 14.3 1.0 CG A:ASP120 4.8 14.8 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