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Atomistry » Magnesium » PDB 2bt6-2c3y » 2bz0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2bt6-2c3y » 2bz0 » |
Magnesium in PDB 2bz0: Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and ZincEnzymatic activity of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc
All present enzymatic activity of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc:
3.5.4.25; Protein crystallography data
The structure of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc, PDB code: 2bz0
was solved by
J.Ren,
M.Kotaka,
M.Lockyer,
H.K.Lamb,
A.R.Hawkins,
D.K.Stammers,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2bz0:
The structure of Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc
(pdb code 2bz0). 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 Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc, PDB code: 2bz0: Magnesium binding site 1 out of 1 in 2bz0Go back to Magnesium Binding Sites List in 2bz0
Magnesium binding site 1 out
of 1 in the Crystal Structure of E. Coli Gtp Cyclohydrolase II in Complex with Gtp Analogue, Gmpcpp, and Zinc
Mono view Stereo pair view
Reference:
J.Ren,
M.Kotaka,
M.Lockyer,
H.K.Lamb,
A.R.Hawkins,
D.K.Stammers.
Gtp Cyclohydrolase II Structure and Mechanism. J.Biol.Chem. V. 280 36912 2005.
Page generated: Mon Dec 14 07:17:59 2020
ISSN: ISSN 0021-9258 PubMed: 16115872 DOI: 10.1074/JBC.M507725200 |
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