Cobalt in PDB 3i11: Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus

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

The structure of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 3i11 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)	40.13 / 1.45
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.087, 61.363, 69.570, 90.00, 93.00, 90.00
R / Rfree (%)	16.2 / 20.4

The binding sites of Cobalt atom in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus (pdb code 3i11). 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, PDB code: 3i11:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co228 b:23.1 occ:1.00 ND1 A:HIS88 2.0 20.8 1.0 O A:HOH346 2.0 29.8 1.0 NE2 A:HIS149 2.0 19.7 1.0 NE2 A:HIS86 2.1 20.6 1.0 O A:HOH418 2.7 37.8 1.0 CE1 A:HIS88 3.0 21.1 1.0 CD2 A:HIS149 3.0 17.6 1.0 CG A:HIS88 3.0 22.2 1.0 CE1 A:HIS149 3.0 21.4 1.0 CE1 A:HIS86 3.0 20.5 1.0 CD2 A:HIS86 3.1 20.1 1.0 CB A:HIS88 3.4 22.7 1.0 CO A:CO229 3.7 28.2 0.5 O A:HOH329 3.9 31.7 0.5 OD1 A:ASP90 3.9 35.0 1.0 NE2 A:HIS88 4.1 22.6 1.0 CD2 A:HIS88 4.1 21.1 1.0 ND1 A:HIS149 4.1 18.8 1.0 ND1 A:HIS86 4.2 18.8 1.0 CG A:HIS149 4.2 16.5 1.0 CG2 A:THR150 4.2 16.9 1.0 CG A:HIS86 4.2 15.8 1.0 CB A:CYS168 4.4 19.4 0.5 SG A:CYS168 4.4 19.2 0.5 CB A:CYS168 4.4 18.3 0.5 SG A:CYS168 4.5 19.3 0.5 CG A:ASP90 4.7 31.4 1.0 OD2 A:ASP90 4.8 35.7 1.0 CA A:HIS88 4.8 22.7 1.0

Cobalt binding site 2 out of 2 in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co229 b:28.2 occ:0.50 SG A:CYS168 1.8 19.2 0.5 O A:HOH329 1.9 31.7 0.5 O A:HOH346 2.3 29.8 1.0 SG A:CYS168 2.3 19.3 0.5 NE2 A:HIS210 2.4 35.9 1.0 OD2 A:ASP90 2.5 35.7 1.0 CB A:CYS168 3.2 19.4 0.5 CB A:CYS168 3.3 18.3 0.5 CD2 A:HIS210 3.3 35.0 1.0 CE1 A:HIS210 3.4 32.2 1.0 CG A:ASP90 3.5 31.4 1.0 OD1 A:ASP90 3.7 35.0 1.0 CO A:CO228 3.7 23.1 1.0 NE2 A:HIS149 4.2 19.7 1.0 CE1 A:HIS86 4.2 20.5 1.0 NE A:ARG91 4.3 19.9 1.0 O A:HOH418 4.3 37.8 1.0 NH2 A:ARG91 4.3 32.0 1.0 NE2 A:HIS86 4.5 20.6 1.0 ND1 A:HIS210 4.5 33.5 1.0 CG A:HIS210 4.5 30.5 1.0 CA A:CYS168 4.5 17.3 0.5 CA A:CYS168 4.5 17.4 0.5 O A:HOH402 4.5 34.1 1.0 CE1 A:HIS149 4.5 21.4 1.0 CZ A:ARG91 4.8 27.4 1.0 CB A:ASP90 4.8 31.4 1.0 N A:CYS168 4.9 17.2 0.5 CD2 A:HIS149 5.0 17.6 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