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Atomistry » Sodium » PDB 4n01-4nji » 4n0j | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 4n01-4nji » 4n0j » |
Sodium in PDB 4n0j: Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A ResolutionEnzymatic activity of Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution
All present enzymatic activity of Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution:
3.2.1.17; Protein crystallography data
The structure of Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution, PDB code: 4n0j
was solved by
R.E.Mcgovern,
P.B.Crowley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4n0j:
The structure of Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution
(pdb code 4n0j). 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 Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution, PDB code: 4n0j: Sodium binding site 1 out of 1 in 4n0jGo back to![]() ![]()
Sodium binding site 1 out
of 1 in the Crystal Structure of Dimethyllysine Hen Egg-White Lysozyme in Complex with SCLX4 at 1.9 A Resolution
![]() Mono view ![]() Stereo pair view
Reference:
R.E.Mcgovern,
B.D.Snarr,
J.A.Lyons,
J.Mcfarlane,
A.L.Whiting,
I.Paci,
F.Hof,
P.B.Crowley.
Structural Study of A Small Molecule Receptor Bound to Dimethyllysine in Lysozyme Chem.Sci. 2015.
Page generated: Mon Oct 7 17:08:41 2024
DOI: 10.1039/C4SC02383H |
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