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Bromine in PDB 5t6n: Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug ArbidolProtein crystallography data
The structure of Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug Arbidol, PDB code: 5t6n
was solved by
R.U.Kadam,
I.A.Wilson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug Arbidol
(pdb code 5t6n). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug Arbidol, PDB code: 5t6n: Jump to Bromine binding site number: 1; 2; 3; Bromine binding site 1 out of 3 in 5t6nGo back to Bromine Binding Sites List in 5t6n
Bromine binding site 1 out
of 3 in the Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug Arbidol
Mono view Stereo pair view
Bromine binding site 2 out of 3 in 5t6nGo back to Bromine Binding Sites List in 5t6n
Bromine binding site 2 out
of 3 in the Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug Arbidol
Mono view Stereo pair view
Bromine binding site 3 out of 3 in 5t6nGo back to Bromine Binding Sites List in 5t6n
Bromine binding site 3 out
of 3 in the Crystal Structure of the A/Hong Kong/1/1968 (H3N2) Influenza Virus Hemagglutinin in Complex with the Antiviral Drug Arbidol
Mono view Stereo pair view
Reference:
R.U.Kadam,
I.A.Wilson.
Structural Basis of Influenza Virus Fusion Inhibition By the Antiviral Drug Arbidol. Proc. Natl. Acad. Sci. V. 114 206 2017U.S.A..
Page generated: Sat Dec 12 02:30:34 2020
ISSN: ESSN 1091-6490 PubMed: 28003465 DOI: 10.1073/PNAS.1617020114 |
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