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Atomistry » Magnesium » PDB 3rr5-3rv4 » 3ruo » |
Magnesium in PDB 3ruo: Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088)Enzymatic activity of Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088)
All present enzymatic activity of Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088):
3.4.22.28; Protein crystallography data
The structure of Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088), PDB code: 3ruo
was solved by
Z.Kaczmarska,
R.Janowski,
L.Costenaro,
B.Coutard,
H.Norder,
B.Canard,
M.Coll,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ruo:
The structure of Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088)
(pdb code 3ruo). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088), PDB code: 3ruo: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3ruoGo back to Magnesium Binding Sites List in 3ruo
Magnesium binding site 1 out
of 2 in the Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088)
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3ruoGo back to Magnesium Binding Sites List in 3ruo
Magnesium binding site 2 out
of 2 in the Complex Structure of Hevb EV93 Main Protease 3C with Rupintrivir (AG7088)
Mono view Stereo pair view
Reference:
L.Costenaro,
Z.Kaczmarska,
C.Arnan,
R.Janowski,
B.Coutard,
M.Sola,
A.E.Gorbalenya,
H.Norder,
B.Canard,
M.Coll.
Structural Basis For Antiviral Inhibition of the Main Protease, 3C, From Human Enterovirus 93. J.Virol. V. 85 10764 2011.
Page generated: Mon Dec 14 08:46:20 2020
ISSN: ISSN 0022-538X PubMed: 21835784 DOI: 10.1128/JVI.05062-11 |
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