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Sodium in PDB 1uxi: Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface

Enzymatic 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: 1uxi 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:

Resolution Low / High (Å) 25.00 / 2.10
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 149.383, 149.383, 113.866, 90.00, 90.00, 90.00
R / Rfree (%) 24.3 / 27.6

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 1uxi). 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 Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface, PDB code: 1uxi:

Sodium binding site 1 out of 1 in 1uxi

Go back to Sodium Binding Sites List in 1uxi
Sodium binding site 1 out of 1 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

A full contact list of Sodium with other atoms in the Na binding site number 1 of Large Improvement in the Thermal Stability of A Tetrameric Malate Dehydrogenase By Single Point Mutations at the Dimer-Dimer Interface within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1312

b:47.4
occ:0.50
O B:HOH2122 2.4 23.1 1.0
O B:HOH2120 3.3 44.4 1.0
CG2 B:THR187 3.8 20.3 1.0
CG B:PRO192 4.2 25.1 1.0
O B:ARG184 4.3 19.9 1.0
O B:GLY190 4.7 25.1 1.0
O B:HOH2121 4.9 42.6 1.0
CD B:PRO192 4.9 25.9 1.0
CB B:PRO192 4.9 25.3 1.0

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.
ISSN: ISSN 0022-2836
PubMed: 15321717
DOI: 10.1016/J.JMB.2004.06.079
Page generated: Sun Oct 6 22:47:37 2024

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