Zinc in PDB 4tyt: Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F

All present enzymatic activity of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F:
3.5.2.6;

The structure of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F, PDB code: 4tyt was solved by J.Brem, S.S.Van Berkel, M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.05 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.079, 61.358, 69.416, 90.00, 93.00, 90.00
R / Rfree (%)	15 / 20.1

The structure of Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F also contains other interesting chemical elements:

Chlorine

(Cl)

6 atoms

The binding sites of Zinc atom in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F (pdb code 4tyt). 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 ML302F, PDB code: 4tyt:
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 ML302F


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 ML302F within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:21.0 occ:1.00 OD1 A:ASP120 2.2 18.8 1.0 NE2 A:HIS240 2.2 17.7 1.0 SG A:CYS198 2.2 16.6 1.0 O8 A:S3C303 2.3 32.4 0.3 O8 A:S3C303 2.3 32.3 0.7 S9 A:S3C303 2.4 17.5 0.7 S9 A:S3C303 2.5 27.0 0.3 C6 A:S3C303 3.0 32.7 0.7 C6 A:S3C303 3.1 31.9 0.3 C5 A:S3C303 3.1 29.4 0.7 CG A:ASP120 3.1 25.1 1.0 CD2 A:HIS240 3.1 17.6 1.0 CE1 A:HIS240 3.2 17.2 1.0 C5 A:S3C303 3.2 30.5 0.3 CB A:CYS198 3.3 16.2 1.0 OD2 A:ASP120 3.5 18.8 1.0 ZN A:ZN302 3.8 15.5 1.0 NH2 A:ARG121 4.0 25.5 1.0 NE A:ARG121 4.1 17.8 1.0 O7 A:S3C303 4.2 31.7 0.7 CE1 A:HIS116 4.2 13.0 1.0 O7 A:S3C303 4.3 31.9 0.3 ND1 A:HIS240 4.3 18.9 1.0 CG A:HIS240 4.3 19.6 1.0 C4 A:S3C303 4.4 28.2 0.7 CB A:ASP120 4.4 21.2 1.0 NE2 A:HIS179 4.4 12.2 1.0 CZ A:ARG121 4.4 25.7 1.0 NE2 A:HIS116 4.4 11.9 1.0 C4 A:S3C303 4.5 29.7 0.3 CL2 A:S3C303 4.5 30.5 0.7 O A:HOH515 4.5 19.4 1.0 CA A:CYS198 4.6 15.4 1.0 CL1 A:S3C303 4.8 30.3 0.3 CE1 A:HIS179 4.9 15.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Bcii Metallo-Beta-Lactamase in Complex with ML302F


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 ML302F within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:15.5 occ:1.00 ND1 A:HIS118 2.0 14.6 1.0 NE2 A:HIS179 2.0 12.2 1.0 NE2 A:HIS116 2.1 11.9 1.0 S9 A:S3C303 2.3 17.5 0.7 S9 A:S3C303 2.3 27.0 0.3 CG A:HIS118 3.0 18.9 1.0 CD2 A:HIS179 3.0 11.1 1.0 CE1 A:HIS116 3.0 13.0 1.0 CE1 A:HIS118 3.0 17.8 1.0 CE1 A:HIS179 3.1 15.3 1.0 CD2 A:HIS116 3.1 14.4 1.0 C5 A:S3C303 3.1 29.4 0.7 C5 A:S3C303 3.2 30.5 0.3 CB A:HIS118 3.3 19.0 1.0 ZN A:ZN301 3.8 21.0 1.0 C6 A:S3C303 3.9 31.9 0.3 C6 A:S3C303 3.9 32.7 0.7 O8 A:S3C303 4.0 32.3 0.7 O8 A:S3C303 4.0 32.4 0.3 C4 A:S3C303 4.0 28.2 0.7 OD2 A:ASP120 4.0 18.8 1.0 C4 A:S3C303 4.1 29.7 0.3 ND1 A:HIS116 4.1 10.7 1.0 NE2 A:HIS118 4.1 15.4 1.0 CD2 A:HIS118 4.1 17.3 1.0 C3 A:S3C303 4.1 27.9 0.7 CG A:HIS179 4.1 11.8 1.0 ND1 A:HIS179 4.1 11.8 1.0 C3 A:S3C303 4.2 30.3 0.3 CG A:HIS116 4.2 10.6 1.0 CB A:CYS198 4.3 16.2 1.0 C2 A:S3C303 4.3 27.0 0.7 CG2 A:THR180 4.3 13.3 1.0 C10 A:S3C303 4.3 27.8 0.3 SG A:CYS198 4.4 16.6 1.0 CL2 A:S3C303 4.5 25.0 0.3 CL1 A:S3C303 4.5 26.3 0.7 C10 A:S3C303 4.7 32.4 0.7 CA A:HIS118 4.7 16.7 1.0 C2 A:S3C303 4.7 32.1 0.3 OD1 A:ASP120 4.8 18.8 1.0 CG A:ASP120 4.8 25.1 1.0 O7 A:S3C303 4.9 31.9 0.3 O7 A:S3C303 5.0 31.7 0.7

J.Brem, S.S.Van Berkel, W.Aik, A.M.Rydzik, M.B.Avison, I.Pettinati, K.-D.Umland, A.Kawamura, J.Spencer, T.D.W.Claridge, M.A.Mcdonough, C.J.Schofield. Rhodanine Hydrolysis Leads to Potent Thioenolate Mediated Metallo-Beta-Lactamase Inhibition Nat.Chem. 2014.
ISSN: ESSN 1755-4349
DOI: 10.1038/NCHEM.2110