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Mercury in PDB 1can: Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate AnionsEnzymatic activity of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions
All present enzymatic activity of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions:
4.2.1.1; Protein crystallography data
The structure of Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions, PDB code: 1can
was solved by
S.Mangani,
K.Hakansson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Mercury Binding Sites:
The binding sites of Mercury atom in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions
(pdb code 1can). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions, PDB code: 1can: Jump to Mercury binding site number: 1; 2; Mercury binding site 1 out of 2 in 1canGo back to Mercury Binding Sites List in 1can
Mercury binding site 1 out
of 2 in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions
Mono view Stereo pair view
Mercury binding site 2 out of 2 in 1canGo back to Mercury Binding Sites List in 1can
Mercury binding site 2 out
of 2 in the Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions
Mono view Stereo pair view
Reference:
S.Mangani,
K.Hakansson.
Crystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors to Carbonic Anhydrase Using Hydrogen Sulphide and Nitrate Anions. Eur.J.Biochem. V. 210 867 1992.
Page generated: Sun Dec 13 19:02:10 2020
ISSN: ISSN 0014-2956 PubMed: 1336460 DOI: 10.1111/J.1432-1033.1992.TB17490.X |
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