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Atomistry » Sodium » PDB 1l0r-1m65 » 1lrk » |
Sodium in PDB 1lrk: Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-AcetylglucosamineEnzymatic activity of Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine
All present enzymatic activity of Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine:
5.1.3.2; Protein crystallography data
The structure of Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine, PDB code: 1lrk
was solved by
J.B.Thoden,
J.M.Henderson,
J.L.Fridovich-Keil,
H.M.Holden,
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 Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine
(pdb code 1lrk). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine, PDB code: 1lrk: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 1lrkGo back to Sodium Binding Sites List in 1lrk
Sodium binding site 1 out
of 2 in the Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 1lrkGo back to Sodium Binding Sites List in 1lrk
Sodium binding site 2 out
of 2 in the Crystal Structure of Escherichia Coli Udp-Galactose 4-Epimerase Mutant Y299C Complexed with Udp-N-Acetylglucosamine
Mono view Stereo pair view
Reference:
J.B.Thoden,
J.M.Henderson,
J.L.Fridovich-Keil,
H.M.Holden.
Structural Analysis of the Y299C Mutant of Escherichia Coli Udp-Galactose 4-Epimerase. Teaching An Old Dog New Tricks. J.Biol.Chem. V. 277 27528 2002.
Page generated: Sun Oct 6 20:17:55 2024
ISSN: ISSN 0021-9258 PubMed: 12019271 DOI: 10.1074/JBC.M204413200 |
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