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Atomistry » Sodium » PDB 6w0s-6wn2 » 6wdu | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 6w0s-6wn2 » 6wdu » |
Sodium in PDB 6wdu: The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring.Enzymatic activity of The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring.
All present enzymatic activity of The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring.:
4.2.1.20; Protein crystallography data
The structure of The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring., PDB code: 6wdu
was solved by
E.Hilario,
L.Fan,
M.F.Dunn,
L.J.Mueller,
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 The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring.
(pdb code 6wdu). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring., PDB code: 6wdu: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 6wduGo back to Sodium Binding Sites List in 6wdu
Sodium binding site 1 out
of 2 in the The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring.
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 6wduGo back to Sodium Binding Sites List in 6wdu
Sodium binding site 2 out
of 2 in the The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring.
Mono view Stereo pair view
Reference:
E.Hilario,
L.Fan,
M.F.Dunn,
L.J.Mueller.
The External Aldimine Form of the Salmonella Thypi Wild-Type Tryptophan Synthase in Open Conformation Showing Multiple Side Chain Conformations For the Residue Beta Q114 and Sodium Ion at the Metal Coordination Site. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring. To Be Published.
Page generated: Tue Oct 8 14:33:29 2024
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