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Atomistry » Sodium » PDB 1x9j-1y4d » 1x9j » |
Sodium in PDB 1x9j: Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational ChangesEnzymatic activity of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes
All present enzymatic activity of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes:
2.7.2.7; Protein crystallography data
The structure of Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes, PDB code: 1x9j
was solved by
J.S.Diao,
D.A.Sanders,
M.S.Hasson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes
(pdb code 1x9j). 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 Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes, PDB code: 1x9j: Sodium binding site 1 out of 1 in 1x9jGo back to Sodium Binding Sites List in 1x9j
Sodium binding site 1 out
of 1 in the Structure of Butyrate Kinase 2 Reveals Both Open- and Citrate-Induced Closed Conformations: Implications For Substrate-Induced Fit Conformational Changes
Mono view Stereo pair view
Reference:
J.S.Diao,
S.Bhattacharyya,
Y.L.D.Ma,
D.A.Sanders,
M.S.Hasson.
Structure of Butyrate Kinase 2 Reveals Both Open and Closed Conformations of the Two Domains: Implications For Substrate-Induced Changes To Be Published.
Page generated: Tue Dec 15 05:41:36 2020
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