Zinc in PDB 1bvt: Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9

All present enzymatic activity of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9:
3.5.2.6;

The structure of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9, PDB code: 1bvt was solved by A.Carfi, 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 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.000, 61.350, 69.450, 90.00, 92.93, 90.00
R / Rfree (%)	22.2 / 26.9

The binding sites of Zinc atom in the Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 (pdb code 1bvt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9, PDB code: 1bvt:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn229 b:25.8 occ:0.60 NE2 A:HIS210 2.2 21.9 1.0 OD2 A:ASP90 2.3 27.6 1.0 SG A:CYS168 2.4 22.9 1.0 O2 A:BCT230 2.9 22.0 0.6 O1 A:BCT230 3.1 23.4 0.6 CG A:ASP90 3.1 24.9 1.0 CD2 A:HIS210 3.1 17.4 1.0 CE1 A:HIS210 3.3 19.4 1.0 C A:BCT230 3.4 22.7 0.6 OD1 A:ASP90 3.4 25.3 1.0 O A:HOH516 3.7 18.1 1.0 CB A:CYS168 3.8 15.5 1.0 ZN A:ZN228 3.8 20.7 1.0 NH2 A:ARG91 4.2 20.1 1.0 CG A:HIS210 4.3 17.4 1.0 NE A:ARG91 4.4 17.3 1.0 CB A:ASP90 4.4 22.4 1.0 ND1 A:HIS210 4.4 18.1 1.0 CE1 A:HIS86 4.5 9.5 1.0 NE2 A:HIS149 4.6 16.1 1.0 NE2 A:HIS86 4.6 9.8 1.0 CZ A:ARG91 4.7 16.5 1.0 O3 A:BCT230 4.7 22.7 0.6 O A:HOH357 4.7 35.3 1.0 CE1 A:HIS149 4.9 15.2 1.0 CA A:CYS168 5.0 12.3 1.0

Zinc binding site 2 out of 2 in the Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo-Beta-Lactamase From Bacillus Cereus 569/H/9 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn228 b:20.7 occ:1.00 O A:HOH516 2.1 18.1 1.0 ND1 A:HIS88 2.2 14.5 1.0 NE2 A:HIS149 2.2 16.1 1.0 NE2 A:HIS86 2.2 9.8 1.0 CD2 A:HIS149 2.9 12.8 1.0 CG A:HIS88 3.1 15.0 1.0 CE1 A:HIS86 3.1 9.5 1.0 CD2 A:HIS86 3.2 7.0 1.0 CE1 A:HIS88 3.2 12.7 1.0 CE1 A:HIS149 3.3 15.2 1.0 CB A:HIS88 3.3 16.0 1.0 ZN A:ZN229 3.8 25.8 0.6 OD1 A:ASP90 3.9 25.3 1.0 CG A:HIS149 4.2 11.9 1.0 ND1 A:HIS86 4.2 7.1 1.0 CD2 A:HIS88 4.2 15.0 1.0 SG A:CYS168 4.2 22.9 1.0 CB A:CYS168 4.3 15.5 1.0 CG A:HIS86 4.3 6.8 1.0 NE2 A:HIS88 4.3 12.9 1.0 ND1 A:HIS149 4.3 9.8 1.0 CG2 A:THR150 4.3 5.7 1.0 O1 A:BCT230 4.5 23.4 0.6 O A:HOH440 4.6 38.1 1.0 O2 A:BCT230 4.7 22.0 0.6 CA A:HIS88 4.8 14.4 1.0 CG A:ASP90 4.8 24.9 1.0 OD2 A:ASP90 4.8 27.6 1.0 C A:BCT230 4.8 22.7 0.6

A.Carfi, E.Duee, M.Galleni, J.M.Frere, O.Dideberg. 1.85 A Resolution Structure of the Zinc (II) Beta-Lactamase From Bacillus Cereus. Acta Crystallogr.,Sect.D V. 54 313 1998.
ISSN: ISSN 0907-4449
PubMed: 9761898
DOI: 10.1107/S0907444997010627