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Atomistry » Sodium » PDB 1l0r-1m65 » 1lk5 » |
Sodium in PDB 1lk5: Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus HorikoshiiEnzymatic activity of Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii
All present enzymatic activity of Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii:
5.3.1.6; Protein crystallography data
The structure of Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii, PDB code: 1lk5
was solved by
K.Ishikawa,
I.Matsui,
F.Payan,
C.Cambillau,
H.Ishida,
Y.Kawarabayasi,
H.Kikuchi,
A.Roussel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1lk5:
The structure of Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii
(pdb code 1lk5). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii, PDB code: 1lk5: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 1lk5Go back to![]() ![]()
Sodium binding site 1 out
of 2 in the Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 2 in 1lk5Go back to![]() ![]()
Sodium binding site 2 out
of 2 in the Structure of the D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii
![]() Mono view ![]() Stereo pair view
Reference:
K.Ishikawa,
I.Matsui,
F.Payan,
C.Cambillau,
H.Ishida,
Y.Kawarabayasi,
H.Kikuchi,
A.Roussel.
A Hyperthermostable D-Ribose-5-Phosphate Isomerase From Pyrococcus Horikoshii Characterization and Three-Dimensional Structure. Structure V. 10 877 2002.
Page generated: Sun Oct 6 20:17:02 2024
ISSN: ISSN 0969-2126 PubMed: 12057201 DOI: 10.1016/S0969-2126(02)00779-7 |
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