Zinc in PDB 1bmc: Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus

All present enzymatic activity of Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus:
3.5.2.6;

The structure of Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 1bmc was solved by A.Carfi, S.Pares, E.Duee, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.790, 61.980, 69.970, 90.00, 93.67, 90.00
R / Rfree (%)	22 / 33

The binding sites of Zinc atom in the Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus (pdb code 1bmc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 1bmc:

Zinc binding site 1 out of 1 in the Structure of A Zinc 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 Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn228 b:24.6 occ:1.00 NE2 A:HIS149 2.4 6.2 1.0 ND1 A:HIS88 2.4 19.9 1.0 NE2 A:HIS86 2.5 8.5 1.0 O A:HOH307 3.3 19.4 1.0 CG A:HIS88 3.3 19.9 1.0 CE1 A:HIS86 3.3 8.5 1.0 CD2 A:HIS149 3.3 6.2 1.0 CE1 A:HIS149 3.4 6.2 1.0 CE1 A:HIS88 3.4 19.9 1.0 CB A:HIS88 3.4 19.9 1.0 CD2 A:HIS86 3.4 8.5 1.0 OD1 A:ASP90 4.0 27.0 1.0 SG A:CYS168 4.3 21.6 1.0 ND1 A:HIS86 4.4 8.5 1.0 CD2 A:HIS88 4.5 19.9 1.0 ND1 A:HIS149 4.5 6.2 1.0 CG A:HIS149 4.5 6.2 1.0 CG A:HIS86 4.5 8.5 1.0 NE2 A:HIS88 4.5 19.9 1.0 CB A:CYS168 4.6 21.6 1.0 OD2 A:ASP90 4.7 27.0 1.0 CG A:ASP90 4.7 27.0 1.0 CA A:HIS88 4.9 18.0 1.0

A.Carfi, S.Pares, E.Duee, M.Galleni, C.Duez, J.M.Frere, O.Dideberg. The 3-D Structure of A Zinc Metallo-Beta-Lactamase From Bacillus Cereus Reveals A New Type of Protein Fold. Embo J. V. 14 4914 1995.
ISSN: ISSN 0261-4189
PubMed: 7588620