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Atomistry » Sodium » PDB 7v8r-7wj2 » 7vgp | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 7v8r-7wj2 » 7vgp » |
Sodium in PDB 7vgp: Hen Egg Lysozyme Refolded After Denaturation at Acidic pHEnzymatic activity of Hen Egg Lysozyme Refolded After Denaturation at Acidic pH
All present enzymatic activity of Hen Egg Lysozyme Refolded After Denaturation at Acidic pH:
3.2.1.17; Protein crystallography data
The structure of Hen Egg Lysozyme Refolded After Denaturation at Acidic pH, PDB code: 7vgp
was solved by
M.Oda,
T.Ikura,
N.Ito,
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 Hen Egg Lysozyme Refolded After Denaturation at Acidic pH
(pdb code 7vgp). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Hen Egg Lysozyme Refolded After Denaturation at Acidic pH, PDB code: 7vgp: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 7vgpGo back to Sodium Binding Sites List in 7vgp
Sodium binding site 1 out
of 2 in the Hen Egg Lysozyme Refolded After Denaturation at Acidic pH
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 7vgpGo back to Sodium Binding Sites List in 7vgp
Sodium binding site 2 out
of 2 in the Hen Egg Lysozyme Refolded After Denaturation at Acidic pH
Mono view Stereo pair view
Reference:
M.Oda,
T.Sano,
Y.O.Kamatari,
Y.Abe,
T.Ikura,
N.Ito.
Structural Analysis of Hen Egg Lysozyme Refolded After Denaturation at Acidic pH. Protein J. V. 41 71 2022.
Page generated: Wed Oct 9 09:19:49 2024
ISSN: ISSN 1572-3887 PubMed: 35094218 DOI: 10.1007/S10930-021-10036-3 |
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