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Magnesium in PDB 3rq2: Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with NadhEnzymatic activity of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis Co-Crystallized with Atp/MG2+ and Soaked with Nadh
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 Nadh:
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 Nadh, PDB code: 3rq2
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 Nadh
(pdb code 3rq2). 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 Nadh, PDB code: 3rq2: Magnesium binding site 1 out of 1 in 3rq2Go back to Magnesium Binding Sites List in 3rq2
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 Nadh
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: Mon Dec 14 08:45:32 2020
ISSN: ISSN 0969-2126 PubMed: 22940582 DOI: 10.1016/J.STR.2012.07.016 |
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