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| Atomistry » Chlorine » PDB 2h9b-2hqk » 2hd6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Atomistry » Chlorine » PDB 2h9b-2hqk » 2hd6 » |
Chlorine in PDB 2hd6: Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide.Enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide.
All present enzymatic activity of Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide.:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide., PDB code: 2hd6
was solved by
G.De Simone,
R.M.Vitale,
A.Di Fiore,
C.Pedone,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2hd6:
The structure of Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide. also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide.
(pdb code 2hd6). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide., PDB code: 2hd6: Chlorine binding site 1 out of 1 in 2hd6Go back to
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Human Carbonic Anhydrase II in Complex with A Hypoxia-Activatable Sulfonamide.
![]() Mono view ![]() Stereo pair view
Reference:
G.De Simone,
R.M.Vitale,
A.Di Fiore,
C.Pedone,
A.Scozzafava,
J.L.Montero,
J.Y.Winum,
C.T.Supuran.
Carbonic Anhydrase Inhibitors: Hypoxia-Activatable Sulfonamides Incorporating Disulfide Bonds That Target the Tumor-Associated Isoform IX. J.Med.Chem. V. 49 5544 2006.
Page generated: Thu Jul 10 22:32:13 2025
ISSN: ISSN 0022-2623 PubMed: 16942027 DOI: 10.1021/JM060531J |
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