Zinc in PDB 6dja: Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus

All present enzymatic activity of Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus:
3.5.2.6;

The structure of Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 6dja was solved by A.A.Bui, N.H.Khan, R.W.Shaw, R.B.Sutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.90 / 2.48
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	71.087, 71.087, 96.182, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 20.9

The binding sites of Zinc atom in the Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus (pdb code 6dja). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 6dja:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:46.7 occ:1.00 NE2 A:HIS179 2.2 26.2 1.0 NE2 A:HIS116 2.2 30.1 1.0 ND1 A:HIS118 2.2 31.9 1.0 O A:HOH428 2.5 42.5 1.0 CD2 A:HIS179 3.0 27.4 1.0 CG A:HIS118 3.1 34.7 1.0 CE1 A:HIS116 3.2 27.9 1.0 CD2 A:HIS116 3.2 30.2 1.0 CE1 A:HIS118 3.3 34.5 1.0 CB A:HIS118 3.3 35.7 1.0 CE1 A:HIS179 3.3 27.2 1.0 OD1 A:ASP120 3.9 40.9 1.0 ZN A:ZN302 4.0 87.1 1.0 CG A:HIS179 4.2 27.1 1.0 ND1 A:HIS116 4.3 27.5 1.0 SG A:CYS198 4.3 41.3 1.0 CD2 A:HIS118 4.3 36.9 1.0 CG A:HIS116 4.3 29.1 1.0 ND1 A:HIS179 4.3 26.5 1.0 NE2 A:HIS118 4.3 36.6 1.0 CB A:CYS198 4.3 33.6 1.0 CG2 A:THR180 4.7 31.0 1.0 OD2 A:ASP120 4.7 39.7 1.0 CA A:HIS118 4.7 38.4 1.0 CG A:ASP120 4.8 37.9 1.0 ND2 A:ASN210 4.8 41.0 1.0

Zinc binding site 2 out of 2 in the Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zn-Dependent 5/B/6 Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:87.1 occ:1.00 SG A:CYS198 1.9 41.3 1.0 O A:HOH428 2.3 42.5 1.0 NE2 A:HIS240 2.6 30.3 0.5 CB A:CYS198 2.7 33.6 1.0 CD2 A:HIS240 3.1 30.4 0.5 CE1 A:HIS240 3.3 30.1 0.5 OD2 A:ASP120 3.7 39.7 1.0 CA A:CYS198 3.8 28.9 1.0 NE2 A:HIS179 3.9 26.2 1.0 ZN A:ZN301 4.0 46.7 1.0 CG A:HIS240 4.1 29.8 0.5 NH2 A:ARG121 4.1 37.0 1.0 ND1 A:HIS240 4.1 30.8 0.5 CE1 A:HIS179 4.2 27.2 1.0 CD2 A:HIS240 4.4 31.3 0.5 CG A:ASP120 4.6 37.9 1.0 CD2 A:HIS179 4.6 27.4 1.0 N A:CYS198 4.6 26.9 1.0 CE1 A:HIS116 4.7 27.9 1.0 OD1 A:ASP120 4.8 40.9 1.0 NE A:ARG121 4.8 38.6 1.0 CA A:GLY239 4.8 23.9 1.0 CZ A:ARG121 4.8 37.7 1.0 O A:HOH432 4.9 29.9 1.0 C A:GLY239 4.9 25.4 1.0 NE2 A:HIS116 5.0 30.1 1.0 ND1 A:HIS179 5.0 26.5 1.0

A.A.Bui, N.H.Khan, B.J.Wylie, R.B.Sutton, M.P.Latham, R.W.Shaw. Allosteric Inhibition of Bacillus Cereus 5/B/6 Beta-Lactamase By Deca-Nucleotide Aptamer To Be Published.