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Atomistry » Potassium » PDB 1yjn-2aaq » 2aaq | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 1yjn-2aaq » 2aaq » |
Potassium in PDB 2aaq: Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with GopiEnzymatic activity of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi
All present enzymatic activity of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi:
1.8.1.7; Protein crystallography data
The structure of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi, PDB code: 2aaq
was solved by
S.Urig,
K.Fritz-Wolf,
R.Reau,
C.Herold-Mende,
K.Toth,
E.Davioud-Charvet,
K.Becker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2aaq:
The structure of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi
(pdb code 2aaq). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi, PDB code: 2aaq: Potassium binding site 1 out of 1 in 2aaqGo back to Potassium Binding Sites List in 2aaq
Potassium binding site 1 out
of 1 in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi
Mono view Stereo pair view
Reference:
S.Urig,
K.Fritz-Wolf,
R.Reau,
C.Herold-Mende,
K.Toth,
E.Davioud-Charvet,
K.Becker.
Undressing of Phosphine Gold(I) Complexes As Irreversible Inhibitors of Human Disulfide Reductases. Angew.Chem.Int.Ed.Engl. V. 45 1881 2006.
Page generated: Sun Dec 13 23:08:40 2020
ISSN: ISSN 1433-7851 PubMed: 16493712 DOI: 10.1002/ANIE.200502756 |
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