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Atomistry » Zinc » PDB 2vqx-2w13 » 2vyo | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2vqx-2w13 » 2vyo » |
Zinc in PDB 2vyo: Chitin Deacetylase Family Member From Encephalitozoon CuniculiEnzymatic activity of Chitin Deacetylase Family Member From Encephalitozoon Cuniculi
All present enzymatic activity of Chitin Deacetylase Family Member From Encephalitozoon Cuniculi:
3.5.1.41; Protein crystallography data
The structure of Chitin Deacetylase Family Member From Encephalitozoon Cuniculi, PDB code: 2vyo
was solved by
J.E.Urch,
R.Hurtado-Guerrero,
C.Texier,
D.M.F.Van Aalten,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2vyo:
The structure of Chitin Deacetylase Family Member From Encephalitozoon Cuniculi also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Chitin Deacetylase Family Member From Encephalitozoon Cuniculi
(pdb code 2vyo). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Chitin Deacetylase Family Member From Encephalitozoon Cuniculi, PDB code: 2vyo: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2vyoGo back to Zinc Binding Sites List in 2vyo
Zinc binding site 1 out
of 2 in the Chitin Deacetylase Family Member From Encephalitozoon Cuniculi
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2vyoGo back to Zinc Binding Sites List in 2vyo
Zinc binding site 2 out
of 2 in the Chitin Deacetylase Family Member From Encephalitozoon Cuniculi
Mono view Stereo pair view
Reference:
J.E.Urch,
R.Hurtado-Guerrero,
D.Brosson,
Z.Liu,
V.G.H.Eijsink,
C.Texier,
D.M.F.Van Aalten.
Structural and Functional Characterization of A Putative Polysaccharide Deacetylase of the Human Parasite Encephalitozoon Cuniculi. Protein Sci. V. 18 1197 2009.
Page generated: Wed Dec 16 03:56:37 2020
ISSN: ISSN 0961-8368 PubMed: 19472335 DOI: 10.1002/PRO.128 |
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