|
Atomistry » Sodium » PDB 1oar-1ph6 » 1oua | |||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1oar-1ph6 » 1oua » |
Sodium in PDB 1oua: Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T MutantEnzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T Mutant
All present enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T Mutant:
3.2.1.17; Protein crystallography data
The structure of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T Mutant, PDB code: 1oua
was solved by
K.Takano,
J.Funahashi,
Y.Yamagata,
K.Ogasahara,
K.Yutani,
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 Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T Mutant
(pdb code 1oua). 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 Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T Mutant, PDB code: 1oua: Sodium binding site 1 out of 1 in 1ouaGo back to Sodium Binding Sites List in 1oua
Sodium binding site 1 out
of 1 in the Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: X-Ray Structure of the I56T Mutant
Mono view Stereo pair view
Reference:
J.Funahashi,
K.Takano,
K.Ogasahara,
Y.Yamagata,
K.Yutani.
The Structure, Stability, and Folding Process of Amyloidogenic Mutant Human Lysozyme. J.Biochem.(Tokyo) V. 120 1216 1996.
Page generated: Sun Oct 6 21:13:18 2024
ISSN: ISSN 0021-924X PubMed: 9010773 |
Last articlesZn in 9JYWZn in 9IR4 Zn in 9IR3 Zn in 9GMX Zn in 9GMW Zn in 9JEJ Zn in 9ERF Zn in 9ERE Zn in 9EGV Zn in 9EGW |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |