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Atomistry » Fluorine » PDB 1mmd-1o5f » 1nel » |
Fluorine in PDB 1nel: Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms ResolutionEnzymatic activity of Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution
All present enzymatic activity of Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution:
4.2.1.11; Protein crystallography data
The structure of Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution, PDB code: 1nel
was solved by
L.Lebioda,
E.Zhang,
K.Lewinski,
M.J.Brewer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1nel:
The structure of Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution
(pdb code 1nel). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution, PDB code: 1nel: Fluorine binding site 1 out of 1 in 1nelGo back to![]() ![]()
Fluorine binding site 1 out
of 1 in the Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-MG2+-F--Pi Complex at 2.6-Angstroms Resolution
![]() Mono view ![]() Stereo pair view
Reference:
L.Lebioda,
E.Zhang,
K.Lewinski,
J.M.Brewer.
Fluoride Inhibition of Yeast Enolase: Crystal Structure of the Enolase-Mg(2+)-F(-)-Pi Complex at 2.6 A Resolution. Proteins V. 16 219 1993.
Page generated: Mon Jul 14 11:21:05 2025
ISSN: ISSN 0887-3585 PubMed: 8346189 DOI: 10.1002/PROT.340160302 |
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