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Atomistry » Magnesium » PDB 3qpp-3r10 » 3qy0 » |
Magnesium in PDB 3qy0: Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with GdpEnzymatic activity of Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp
All present enzymatic activity of Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp:
6.3.3.3; Protein crystallography data
The structure of Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp, PDB code: 3qy0
was solved by
P.J.Porebski,
M.M.Klimecka,
M.Chruszcz,
K.Murzyn,
A.Joachimiak,
W.Minor,
Midwest Center For Structural Genomics (Mcsg),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp
(pdb code 3qy0). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp, PDB code: 3qy0: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3qy0Go back to![]() ![]()
Magnesium binding site 1 out
of 2 in the Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp
![]() Mono view ![]() Stereo pair view
Magnesium binding site 2 out of 2 in 3qy0Go back to![]() ![]()
Magnesium binding site 2 out
of 2 in the Crystal Structure of Dethiobiotin Synthetase (Biod) From Helicobacter Pylori Complexed with Gdp
![]() Mono view ![]() Stereo pair view
Reference:
P.J.Porebski,
M.Klimecka,
M.Chruszcz,
R.A.Nicholls,
K.Murzyn,
M.E.Cuff,
X.Xu,
M.Cymborowski,
G.N.Murshudov,
A.Savchenko,
A.Edwards,
W.Minor.
Structural Characterization of Helicobacter Pylori Dethiobiotin Synthetase Reveals Differences Between Family Members. Febs J. V. 279 1093 2012.
Page generated: Thu Aug 15 10:13:43 2024
ISSN: ISSN 1742-464X PubMed: 22284390 DOI: 10.1111/J.1742-4658.2012.08506.X |
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