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Atomistry » Sodium » PDB 2bii-2c8x » 2bpu » |
Sodium in PDB 2bpu: The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous DiffractionEnzymatic activity of The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction
All present enzymatic activity of The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction:
3.2.1.17; Protein crystallography data
The structure of The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction, PDB code: 2bpu
was solved by
J.Jakoncic,
M.Di Michiel,
Z.Zhong,
V.Honkimaki,
Y.Jouanneau,
V.Stojanoff,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2bpu:
The structure of The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction
(pdb code 2bpu). 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 The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction, PDB code: 2bpu: Sodium binding site 1 out of 1 in 2bpuGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the The Kedge Holmium Derivative of Hen Egg-White Lysozyme at High Resolution From Single Wavelength Anomalous Diffraction
![]() Mono view ![]() Stereo pair view
Reference:
J.Jakoncic,
M.Di Michiel,
Z.Zhong,
V.Honkimaki,
Y.Jouanneau,
V.Stojanoff.
Anomalous Diffraction at Ultra-High Energy For Protein Crystallography. J.Appl.Crystallogr. V. 39 831 2006.
Page generated: Mon Oct 7 02:01:24 2024
ISSN: ISSN 0021-8898 DOI: 10.1107/S0021889806036387 |
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