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Atomistry » Sodium » PDB 131d-1b7r » 1b5u | ||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 131d-1b7r » 1b5u » |
Sodium in PDB 1b5u: Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala MutantEnzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant
All present enzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant:
3.2.1.17; Protein crystallography data
The structure of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant, PDB code: 1b5u
was solved by
K.Takano,
Y.Yamagata,
M.Kubota,
J.Funahashi,
S.Fujii,
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 Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant
(pdb code 1b5u). 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 Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant, PDB code: 1b5u: Sodium binding site 1 out of 1 in 1b5uGo back to Sodium Binding Sites List in 1b5u
Sodium binding site 1 out
of 1 in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser->Ala Mutant
Mono view Stereo pair view
Reference:
K.Takano,
Y.Yamagata,
M.Kubota,
J.Funahashi,
S.Fujii,
K.Yutani.
Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Ser --> Ala Mutants. Biochemistry V. 38 6623 1999.
Page generated: Sun Oct 6 17:53:04 2024
ISSN: ISSN 0006-2960 PubMed: 10350481 DOI: 10.1021/BI9901228 |
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