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Atomistry » Sodium » PDB 1y5y-1z1q » 1yan | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 1y5y-1z1q » 1yan » |
Sodium in PDB 1yan: Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine MutantsEnzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants
All present enzymatic activity of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants:
3.2.1.17; Protein crystallography data
The structure of Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants, PDB code: 1yan
was solved by
Y.Yamagata,
H.Kaneda,
S.Fujii,
K.Takano,
K.Ogasahara,
E.Kanaya,
M.Kikuchi,
M.Oobatake,
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: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants
(pdb code 1yan). 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: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants, PDB code: 1yan: Sodium binding site 1 out of 1 in 1yanGo back to Sodium Binding Sites List in 1yan
Sodium binding site 1 out
of 1 in the Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants
Mono view Stereo pair view
Reference:
K.Takano,
K.Ogasahara,
H.Kaneda,
Y.Yamagata,
S.Fujii,
E.Kanaya,
M.Kikuchi,
M.Oobatake,
K.Yutani.
Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants. J.Mol.Biol. V. 254 62 1995.
Page generated: Tue Dec 15 05:42:13 2020
ISSN: ISSN 0022-2836 PubMed: 7473760 DOI: 10.1006/JMBI.1995.0599 |
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