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Magnesium in PDB 3rpz: Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with NadphEnzymatic activity of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadph
All present enzymatic activity of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadph:
4.2.1.93; Protein crystallography data
The structure of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadph, PDB code: 3rpz
was solved by
I.A.Shumilin,
M.Cymborowski,
A.Joachimiak,
W.Minor,
Midwest Center Forstructural 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 Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadph
(pdb code 3rpz). 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 Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadph, PDB code: 3rpz: Magnesium binding site 1 out of 1 in 3rpzGo back to Magnesium Binding Sites List in 3rpz
Magnesium binding site 1 out
of 1 in the Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadph
Mono view Stereo pair view
Reference:
I.A.Shumilin,
M.Cymborowski,
O.Chertihin,
K.N.Jha,
J.C.Herr,
S.A.Lesley,
A.Joachimiak,
W.Minor.
Identification of Unknown Protein Function Using Metabolite Cocktail Screening. Structure V. 20 1715 2012.
Page generated: Thu Aug 15 10:33:16 2024
ISSN: ISSN 0969-2126 PubMed: 22940582 DOI: 10.1016/J.STR.2012.07.016 |
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