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Atomistry » Chlorine » PDB 1wbo-1wve » 1wqo » |
Chlorine in PDB 1wqo: Contribution of Hydrogen Bonds to the Conformational Stability of Human LysozymeEnzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme
All present enzymatic activity of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme:
3.2.1.17; Protein crystallography data
The structure of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme, PDB code: 1wqo
was solved by
Y.Yamagata,
M.Kubota,
Y.Sumikawa,
J.Funahashi,
S.Fujii,
K.Yutani,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1wqo:
The structure of Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme
(pdb code 1wqo). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme, PDB code: 1wqo: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 1wqoGo back to Chlorine Binding Sites List in 1wqo
Chlorine binding site 1 out
of 2 in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 1wqoGo back to Chlorine Binding Sites List in 1wqo
Chlorine binding site 2 out
of 2 in the Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme
Mono view Stereo pair view
Reference:
Y.Yamagata,
M.Kubota,
Y.Sumikawa,
J.Funahashi,
K.Takano,
S.Fujii,
K.Yutani.
Contribution of Hydrogen Bonds to the Conformational Stability of Human Lysozyme: Calorimetry and X-Ray Analysis of Six Tyrosine --> Phenylalanine Mutants. Biochemistry V. 37 9355 1998.
Page generated: Sat Dec 12 08:53:57 2020
ISSN: ISSN 0006-2960 PubMed: 9649316 DOI: 10.1021/BI980431I |
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