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Atomistry » Calcium » PDB 5ekk-5eyh » 5enl » |
Calcium in PDB 5enl: Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms ResolutionEnzymatic activity of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution
All present enzymatic activity of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution:
4.2.1.11; Protein crystallography data
The structure of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution, PDB code: 5enl
was solved by
L.Lebioda,
B.Stec,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution
(pdb code 5enl). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution, PDB code: 5enl: Calcium binding site 1 out of 1 in 5enlGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution
![]() Mono view ![]() Stereo pair view
Reference:
L.Lebioda,
B.Stec,
J.M.Brewer,
E.Tykarska.
Inhibition of Enolase: the Crystal Structures of Enolase-CA2(+)- 2-Phosphoglycerate and Enolase-ZN2(+)-Phosphoglycolate Complexes at 2.2-A Resolution. Biochemistry V. 30 2823 1991.
Page generated: Sun Jul 14 18:40:47 2024
ISSN: ISSN 0006-2960 PubMed: 2007121 DOI: 10.1021/BI00225A013 |
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