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Atomistry » Magnesium » PDB 208d-2a6e » 2a5f | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 208d-2a6e » 2a5f » |
Magnesium in PDB 2a5f: Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6Enzymatic activity of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6
All present enzymatic activity of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6:
2.4.2.36; Protein crystallography data
The structure of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6, PDB code: 2a5f
was solved by
C.J.O'neal,
M.G.Jobling,
R.K.Holmes,
W.G.J.Hol,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2a5f:
The structure of Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6
(pdb code 2a5f). 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 Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6, PDB code: 2a5f: Magnesium binding site 1 out of 1 in 2a5fGo back to Magnesium Binding Sites List in 2a5f
Magnesium binding site 1 out
of 1 in the Cholera Toxin A1 Subunit Bound to Its Substrate, Nad+, and Its Human Protein Activator, ARF6
Mono view Stereo pair view
Reference:
C.J.O'neal,
M.G.Jobling,
R.K.Holmes,
W.G.Hol.
Structural Basis For the Activation of Cholera Toxin By Human ARF6-Gtp. Science V. 309 1093 2005.
Page generated: Tue Aug 13 20:22:45 2024
ISSN: ISSN 0036-8075 PubMed: 16099990 DOI: 10.1126/SCIENCE.1113398 |
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