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Atomistry » Sodium » PDB 1ubs-1v54 » 1uxk | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1ubs-1v54 » 1uxk » |
Sodium in PDB 1uxk: Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer InterfaceEnzymatic activity of Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
All present enzymatic activity of Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface:
1.1.1.37; Protein crystallography data
The structure of Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface, PDB code: 1uxk
was solved by
A.Bjork,
B.Dalhus,
D.Mantzilas,
V.G.H.Eijsink,
R.Sirevag,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1uxk:
The structure of Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
(pdb code 1uxk). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 6 binding sites of Sodium where determined in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface, PDB code: 1uxk: Jump to Sodium binding site number: 1; 2; 3; 4; 5; 6; Sodium binding site 1 out of 6 in 1uxkGo back to Sodium Binding Sites List in 1uxk
Sodium binding site 1 out
of 6 in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
Mono view Stereo pair view
Sodium binding site 2 out of 6 in 1uxkGo back to Sodium Binding Sites List in 1uxk
Sodium binding site 2 out
of 6 in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
Mono view Stereo pair view
Sodium binding site 3 out of 6 in 1uxkGo back to Sodium Binding Sites List in 1uxk
Sodium binding site 3 out
of 6 in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
Mono view Stereo pair view
Sodium binding site 4 out of 6 in 1uxkGo back to Sodium Binding Sites List in 1uxk
Sodium binding site 4 out
of 6 in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
Mono view Stereo pair view
Sodium binding site 5 out of 6 in 1uxkGo back to Sodium Binding Sites List in 1uxk
Sodium binding site 5 out
of 6 in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
Mono view Stereo pair view
Sodium binding site 6 out of 6 in 1uxkGo back to Sodium Binding Sites List in 1uxk
Sodium binding site 6 out
of 6 in the Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface
Mono view Stereo pair view
Reference:
A.Bjork,
B.Dalhus,
D.Mantzilas,
R.Sirevag,
V.G.H.Eijsink.
Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface. J.Mol.Biol. V. 341 1215 2004.
Page generated: Sun Oct 6 22:48:01 2024
ISSN: ISSN 0022-2836 PubMed: 15321717 DOI: 10.1016/J.JMB.2004.06.079 |
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