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Atomistry » Cobalt » PDB 3ges-3igy » 3i15 » |
Cobalt in PDB 3i15: Cobalt-Substituted Metallo-Beta-Lactamase From Bacillus Cereus: Residue CYS168 Fully OxidizedEnzymatic 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:
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 3i15Go 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
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.
Page generated: Sun Dec 13 10:40:44 2020
ISSN: ISSN 0006-2960 PubMed: 20677753 DOI: 10.1021/BI100894R |
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