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Atomistry » Sodium » PDB 6dq0-6e8t » 6dv0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 6dq0-6e8t » 6dv0 » |
Sodium in PDB 6dv0: Hiv-1 Wild Type Protease with Grl-02815A, A Thiochroman Heterocycle with (S)-Boc-Amine Functionality As the P2 LigandProtein crystallography data
The structure of Hiv-1 Wild Type Protease with Grl-02815A, A Thiochroman Heterocycle with (S)-Boc-Amine Functionality As the P2 Ligand, PDB code: 6dv0
was solved by
Y.-F.Wang,
J.Agniswamy,
I.T.Weber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6dv0:
The structure of Hiv-1 Wild Type Protease with Grl-02815A, A Thiochroman Heterocycle with (S)-Boc-Amine Functionality As the P2 Ligand also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Hiv-1 Wild Type Protease with Grl-02815A, A Thiochroman Heterocycle with (S)-Boc-Amine Functionality As the P2 Ligand
(pdb code 6dv0). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Hiv-1 Wild Type Protease with Grl-02815A, A Thiochroman Heterocycle with (S)-Boc-Amine Functionality As the P2 Ligand, PDB code: 6dv0: Sodium binding site 1 out of 1 in 6dv0Go back to Sodium Binding Sites List in 6dv0
Sodium binding site 1 out
of 1 in the Hiv-1 Wild Type Protease with Grl-02815A, A Thiochroman Heterocycle with (S)-Boc-Amine Functionality As the P2 Ligand
Mono view Stereo pair view
Reference:
A.K.Ghosh,
R.D.Jadhav,
H.Simpson,
S.Kovela,
H.Osswald,
J.Agniswamy,
Y.F.Wang,
S.I.Hattori,
I.T.Weber,
H.Mitsuya.
Design, Synthesis, and X-Ray Studies of Potent Hiv-1 Protease Inhibitors Incorporating Aminothiochromane and Aminotetrahydronaphthalene Carboxamide Derivatives As the P2 Ligands. Eur J Med Chem V. 160 171 2018.
Page generated: Tue Oct 8 07:46:16 2024
ISSN: ISSN 1768-3254 PubMed: 30340140 DOI: 10.1016/J.EJMECH.2018.09.046 |
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