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Atomistry » Zinc » PDB 1rae-1rpj » 1rk5 » |
Zinc in PDB 1rk5: The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2Enzymatic activity of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2
All present enzymatic activity of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2:
3.5.1.81; Protein crystallography data
The structure of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2, PDB code: 1rk5
was solved by
W.L.Lai,
L.Y.Chou,
C.Y.Ting,
Y.C.Tsai,
S.H.Liaw,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1rk5:
The structure of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2
(pdb code 1rk5). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2, PDB code: 1rk5: Zinc binding site 1 out of 1 in 1rk5Go back to![]() ![]()
Zinc binding site 1 out
of 1 in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2
![]() Mono view ![]() Stereo pair view
Reference:
W.L.Lai,
L.Y.Chou,
C.Y.Ting,
R.Kirby,
Y.C.Tsai,
A.H.Wang,
S.H.Liaw.
The Functional Role of the Binuclear Metal Center in D-Aminoacylase: One-Metal Activation and Second-Metal Attenuation. J.Biol.Chem. V. 279 13962 2004.
Page generated: Mon Jan 25 16:12:43 2021
ISSN: ISSN 0021-9258 PubMed: 14736882 DOI: 10.1074/JBC.M308849200 |
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