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Atomistry » Magnesium » PDB 1h7u-1hxa » 1hpm » |
Magnesium in PDB 1hpm: How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active SiteEnzymatic activity of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site
All present enzymatic activity of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site:
3.6.1.3; Protein crystallography data
The structure of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site, PDB code: 1hpm
was solved by
S.M.Wilbanks,
D.B.Mckay,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1hpm:
The structure of How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site
(pdb code 1hpm). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site, PDB code: 1hpm: Magnesium binding site 1 out of 1 in 1hpmGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site
![]() Mono view ![]() Stereo pair view
Reference:
S.M.Wilbanks,
D.B.Mckay.
How Potassium Affects the Activity of the Molecular Chaperone HSC70. II. Potassium Binds Specifically in the Atpase Active Site. J.Biol.Chem. V. 270 2251 1995.
Page generated: Tue Aug 13 04:00:56 2024
ISSN: ISSN 0021-9258 PubMed: 7836458 DOI: 10.1074/JBC.270.5.2251 |
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