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Atomistry » Sodium » PDB 5v0e-5vb8 » 5v9f | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 5v0e-5vb8 » 5v9f » |
Sodium in PDB 5v9f: Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp.Enzymatic activity of Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp.
All present enzymatic activity of Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp.:
4.1.1.32; Protein crystallography data
The structure of Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp., PDB code: 5v9f
was solved by
T.Holyoak,
D.S.Cui,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5v9f:
The structure of Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp. also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp.
(pdb code 5v9f). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp., PDB code: 5v9f: Sodium binding site 1 out of 1 in 5v9fGo back to Sodium Binding Sites List in 5v9f
Sodium binding site 1 out
of 1 in the Structure of the H477R Variant of Rat Cytosolic Pepck in Complex with Beta Sulfopyruvate and Gtp.
Mono view Stereo pair view
Reference:
D.S.Cui,
A.Broom,
M.J.Mcleod,
E.M.Meiering,
T.Holyoak.
Asymmetric Anchoring Is Required For Efficient Omega-Loop Opening and Closing in Cytosolic Phosphoenolpyruvate Carboxykinase. Biochemistry V. 56 2106 2017.
Page generated: Tue Oct 8 00:46:19 2024
ISSN: ISSN 1520-4995 PubMed: 28345895 DOI: 10.1021/ACS.BIOCHEM.7B00178 |
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