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Magnesium in PDB 3rqq: Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis in Complex with P1,P3-Di(Adenosine-5') TriphosphateEnzymatic activity of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis in Complex with P1,P3-Di(Adenosine-5') Triphosphate
All present enzymatic activity of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis in Complex with P1,P3-Di(Adenosine-5') Triphosphate:
4.2.1.93; Protein crystallography data
The structure of Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis in Complex with P1,P3-Di(Adenosine-5') Triphosphate, PDB code: 3rqq
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 in Complex with P1,P3-Di(Adenosine-5') Triphosphate
(pdb code 3rqq). 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 in Complex with P1,P3-Di(Adenosine-5') Triphosphate, PDB code: 3rqq: Magnesium binding site 1 out of 1 in 3rqqGo back to Magnesium Binding Sites List in 3rqq
Magnesium binding site 1 out
of 1 in the Crystal Structure of Adp/Atp-Dependent Nad(P)H-Hydrate Dehydratase From Bacillus Subtilis in Complex with P1,P3-Di(Adenosine-5') Triphosphate
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 08:45:41 2020
ISSN: ISSN 0969-2126 PubMed: 22940582 DOI: 10.1016/J.STR.2012.07.016 |
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