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Atomistry » Mercury » PDB 3bl0-3k7k » 3ibi » |
Mercury in PDB 3ibi: The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate InhibitorEnzymatic activity of The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor
All present enzymatic activity of The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor:
4.2.1.1; Protein crystallography data
The structure of The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor, PDB code: 3ibi
was solved by
V.Alterio,
G.De Simone,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ibi:
The structure of The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor also contains other interesting chemical elements:
Mercury Binding Sites:
The binding sites of Mercury atom in the The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor
(pdb code 3ibi). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor, PDB code: 3ibi: Mercury binding site 1 out of 1 in 3ibiGo back to Mercury Binding Sites List in 3ibi
Mercury binding site 1 out
of 1 in the The Crystal Structure of the Human Carbonic Anhydrase II in Complex with An Aliphatic Sulfamate Inhibitor
Mono view Stereo pair view
Reference:
R.M.Vitale,
V.Alterio,
A.Innocenti,
J.-Y.Winum,
S.M.Monti,
G.De Simone,
C.T.Supuran.
Carbonic Anhydrase Inhibitors. Comparison of Aliphatic Sulfamate/Bis-Sulfamate Adducts with Isozymes II and IX As A Platform For Designing Tight-Binding, More Isoform-Selective Inhibitors J.Med.Chem. V. 52 5990 2009.
Page generated: Sun Aug 11 03:47:55 2024
ISSN: ISSN 0022-2623 PubMed: 19731956 DOI: 10.1021/JM900641R |
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