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Cobalt in PDB 3i15: Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully Oxidized

Enzymatic activity of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully Oxidized

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

Protein crystallography data

The structure of Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully Oxidized, PDB code: 3i15 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) 40.29 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 53.188, 61.822, 69.521, 90.00, 93.24, 90.00
R / Rfree (%) 15.1 / 18.6

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully Oxidized (pdb code 3i15). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully Oxidized, PDB code: 3i15:

Cobalt binding site 1 out of 1 in 3i15

Go back to Cobalt Binding Sites List in 3i15
Cobalt binding site 1 out of 1 in the Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully 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 Fully Oxidized within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co228

b:24.2
occ:1.00
 NE2 A:HIS149 2.1 12.7 1.0
NE2 A:HIS86 2.1 13.2 1.0
O A:HOH404 2.1 23.4 1.0
ND1 A:HIS88 2.1 15.7 1.0
O A:HOH341 2.2 26.1 1.0
OD1 A:OCS168 2.5 24.8 1.0
CE1 A:HIS149 3.0 14.8 1.0
CE1 A:HIS86 3.0 14.7 1.0
CE1 A:HIS88 3.0 14.9 1.0
CD2 A:HIS149 3.1 12.3 1.0
CD2 A:HIS86 3.1 14.3 1.0
CG A:HIS88 3.2 14.0 1.0
CB A:HIS88 3.6 15.3 1.0
OD2 A:ASP90 3.7 27.3 0.5
SG A:OCS168 3.8 17.3 1.0
CB A:OCS168 4.1 13.8 1.0
ND1 A:HIS149 4.1 12.8 1.0
ND1 A:HIS86 4.2 15.5 1.0
O A:HOH426 4.2 35.8 1.0
CG A:HIS149 4.2 10.9 1.0
NE2 A:HIS88 4.2 15.3 1.0
CG A:HIS86 4.2 12.1 1.0
CD2 A:HIS88 4.3 16.7 1.0
OD3 A:OCS168 4.4 21.4 1.0
O A:HOH393 4.4 31.0 1.0
CG A:ASP90 4.5 24.1 0.5
OD1 A:ASP90 4.5 19.5 0.5
CG2 A:THR150 4.6 10.4 1.0
OD2 A:OCS168 4.7 22.6 1.0

Reference:

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
Page generated: Sun Jul 13 19:00:55 2025

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