Cobalt in PDB 3i14: Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized

All present enzymatic activity of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized:
3.5.2.6;

The structure of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized, PDB code: 3i14 was solved by J.M.Gonzalez, A.Buschiazzo, A.J.Vila, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.44 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.078, 61.699, 69.630, 90.00, 93.09, 90.00
R / Rfree (%)	15.7 / 19.1

The binding sites of Cobalt atom in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized (pdb code 3i14). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized, PDB code: 3i14:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized within 5.0Å range: probe atom residue distance (Å) B Occ A:Co228 b:25.6 occ:1.00 O A:HOH405 1.9 18.4 0.5 ND1 A:HIS88 2.1 15.1 1.0 NE2 A:HIS149 2.1 13.2 1.0 NE2 A:HIS86 2.1 15.2 1.0 O A:HOH405 2.2 18.4 0.5 O A:HOH333 2.4 25.3 1.0 OD1 A:CYS168 2.5 23.3 0.5 CE1 A:HIS88 3.0 16.7 1.0 CE1 A:HIS86 3.0 14.5 1.0 CE1 A:HIS149 3.1 16.1 1.0 CD2 A:HIS149 3.1 13.9 1.0 CD2 A:HIS86 3.1 13.7 1.0 CG A:HIS88 3.1 14.5 1.0 CB A:HIS88 3.5 14.2 1.0 OD1 A:ASP90 3.7 21.8 0.5 CO A:CO229 3.7 25.1 0.5 SG A:CYS168 3.8 19.0 0.5 CB A:CYS168 4.1 15.5 0.5 ND1 A:HIS86 4.1 16.2 1.0 NE2 A:HIS88 4.2 15.4 1.0 ND1 A:HIS149 4.2 11.9 1.0 CG A:HIS149 4.2 10.9 1.0 CB A:CYS168 4.2 12.5 0.5 CG A:HIS86 4.2 12.3 1.0 CD2 A:HIS88 4.2 16.4 1.0 SG A:CYS168 4.3 14.4 0.5 O2 A:GOL230 4.3 42.5 1.0 O3 A:GOL230 4.3 48.6 1.0 C2 A:GOL230 4.4 48.6 1.0 OD2 A:ASP90 4.4 13.1 0.5 O A:HOH427 4.4 36.1 1.0 CG A:ASP90 4.5 20.4 0.5 OD3 A:CYS168 4.5 23.1 0.5 CG2 A:THR150 4.5 11.0 1.0 OD2 A:CYS168 4.8 22.6 0.5 C3 A:GOL230 4.9 48.6 1.0 CA A:HIS88 5.0 15.3 0.5 CA A:HIS88 5.0 13.9 0.5

Cobalt binding site 2 out of 2 in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Partially Oxidized within 5.0Å range: probe atom residue distance (Å) B Occ A:Co229 b:25.1 occ:0.50 OD1 A:CYS168 1.5 23.3 0.5 OD2 A:CYS168 2.0 22.6 0.5 SG A:CYS168 2.0 19.0 0.5 OD2 A:ASP90 2.2 13.1 0.5 O A:HOH405 2.2 18.4 0.5 O2 A:GOL230 2.3 42.5 1.0 O3 A:GOL230 2.3 48.6 1.0 NE2 A:HIS210 2.3 24.7 1.0 SG A:CYS168 2.3 14.4 0.5 OD3 A:CYS168 2.7 23.1 0.5 C3 A:GOL230 3.0 48.6 1.0 C2 A:GOL230 3.0 48.6 1.0 O A:HOH405 3.1 18.4 0.5 CD2 A:HIS210 3.2 21.6 1.0 CG A:ASP90 3.2 20.4 0.5 CE1 A:HIS210 3.4 23.9 1.0 CB A:CYS168 3.5 12.5 0.5 CB A:CYS168 3.6 15.5 0.5 OD1 A:ASP90 3.7 21.8 0.5 CO A:CO228 3.7 25.6 1.0 O A:HOH333 3.8 25.3 1.0 CG A:HIS210 4.4 18.6 1.0 NE A:ARG91 4.4 14.6 1.0 C1 A:GOL230 4.4 50.0 1.0 NE2 A:HIS149 4.4 13.2 1.0 O A:HOH353 4.4 25.6 1.0 NH2 A:ARG91 4.4 25.2 1.0 CB A:ASP90 4.4 19.4 0.5 ND1 A:HIS210 4.5 25.2 1.0 CE1 A:HIS86 4.5 14.5 1.0 CE1 A:HIS149 4.6 16.1 1.0 CA A:CYS168 4.6 14.4 0.5 NE2 A:HIS86 4.7 15.2 1.0 O A:HOH391 4.7 27.7 1.0 CA A:CYS168 4.7 12.3 0.5 CZ A:ARG91 4.9 20.3 1.0

J.M.Gonzalez, A.Buschiazzo, A.J.Vila. Evidence of Adaptability in Metal Coordination Geometry and Active-Site Loop Conformation Among B1 Metallo-Beta-Lactamases . Biochemistry V. 49 7930 2010.
ISSN: ISSN 0006-2960
PubMed: 20677753
DOI: 10.1021/BI100894R